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O00410 (IPO5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:IPO5
Synonyms:KPNB3, RANBP5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1097 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Nucleusnucleolus. 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

Keywords
   Biological processHost-virus interaction
Protein transport
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNLS-bearing protein import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to amino acid stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of catalytic activity

Traceable author statement Ref.2. Source: GOC

positive regulation of protein import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

ribosomal protein import into nucleus

Inferred from direct assay Ref.8. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nuclear membrane

Inferred from direct assay. Source: HPA

nuclear pore

Traceable author statement Ref.2. Source: ProtInc

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGTPase inhibitor activity

Traceable author statement Ref.2. Source: ProtInc

Ran GTPase binding

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 15282309PubMed 22730302. Source: UniProtKB

protein transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 10971096Importin-5
PRO_0000120771

Regions

Domain28 – 9972Importin N-terminal
Repeat212 – 24938HEAT 1
Repeat395 – 43238HEAT 2
Repeat437 – 47539HEAT 3
Repeat859 – 89739HEAT 4
Repeat901 – 93838HEAT 5
Repeat942 – 97938HEAT 6
Region325 – 37551Ran-GTP binding By similarity
Compositional bias2 – 65Poly-Ala
Compositional bias460 – 4656Poly-Ala

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.13 Ref.17 Ref.18
Modified residue8271Phosphoserine Ref.9 Ref.11 Ref.12 Ref.14 Ref.15

Natural variations

Alternative sequence1 – 6060Missing in isoform 2.
VSP_037587
Alternative sequence11M → MPEDQVGKLEATENTISAM in isoform 3.
VSP_037774
Natural variant2861L → I.
Corresponds to variant rs1053814 [ dbSNP | Ensembl ].
VAR_012029
Natural variant5251E → K.
Corresponds to variant rs632729 [ dbSNP | Ensembl ].
VAR_012030
Natural variant5491E → K.
Corresponds to variant rs484770 [ dbSNP | Ensembl ].
VAR_012031
Natural variant9051Y → C.
Corresponds to variant rs1804740 [ dbSNP | Ensembl ].
VAR_012032
Natural variant9691T → I.
Corresponds to variant rs1804741 [ dbSNP | Ensembl ].
VAR_012033

Experimental info

Sequence conflict5381L → R in AAH45640. Ref.6
Sequence conflict826 – 8272ES → GT in AAC51317. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 1864AD23513F2DE1

FASTA1,097123,630
        10         20         30         40         50         60 
MAAAAAEQQQ FYLLLGNLLS PDNVVRKQAE ETYENIPGQS KITFLLQAIR NTTAAEEARQ 

        70         80         90        100        110        120 
MAAVLLRRLL SSAFDEVYPA LPSDVQTAIK SELLMIIQME TQSSMRKKVC DIAAELARNL 

       130        140        150        160        170        180 
IDEDGNNQWP EGLKFLFDSV SSQNVGLREA ALHIFWNFPG IFGNQQQHYL DVIKRMLVQC 

       190        200        210        220        230        240 
MQDQEHPSIR TLSARATAAF ILANEHNVAL FKHFADLLPG FLQAVNDSCY QNDDSVLKSL 

       250        260        270        280        290        300 
VEIADTVPKY LRPHLEATLQ LSLKLCGDTS LNNMQRQLAL EVIVTLSETA AAMLRKHTNI 

       310        320        330        340        350        360 
VAQTIPQMLA MMVDLEEDED WANADELEDD DFDSNAVAGE SALDRMACGL GGKLVLPMIK 

       370        380        390        400        410        420 
EHIMQMLQNP DWKYRHAGLM ALSAIGEGCH QQMEGILNEI VNFVLLFLQD PHPRVRYAAC 

       430        440        450        460        470        480 
NAVGQMATDF APGFQKKFHE KVIAALLQTM EDQGNQRVQA HAAAALINFT EDCPKSLLIP 

       490        500        510        520        530        540 
YLDNLVKHLH SIMVLKLQEL IQKGTKLVLE QVVTSIASVA DTAEEKFVPY YDLFMPSLKH 

       550        560        570        580        590        600 
IVENAVQKEL RLLRGKTIEC ISLIGLAVGK EKFMQDASDV MQLLLKTQTD FNDMEDDDPQ 

       610        620        630        640        650        660 
ISYMISAWAR MCKILGKEFQ QYLPVVMGPL MKTASIKPEV ALLDTQDMEN MSDDDGWEFV 

       670        680        690        700        710        720 
NLGDQQSFGI KTAGLEEKST ACQMLVCYAK ELKEGFVEYT EQVVKLMVPL LKFYFHDGVR 

       730        740        750        760        770        780 
VAAAESMPLL LECARVRGPE YLTQMWHFMC DALIKAIGTE PDSDVLSEIM HSFAKCIEVM 

       790        800        810        820        830        840 
GDGCLNNEHF EELGGILKAK LEEHFKNQEL RQVKRQDEDY DEQVEESLQD EDDNDVYILT 

       850        860        870        880        890        900 
KVSDILHSIF SSYKEKVLPW FEQLLPLIVN LICPHRPWPD RQWGLCIFDD VIEHCSPASF 

       910        920        930        940        950        960 
KYAEYFLRPM LQYVCDNSPE VRQAAAYGLG VMAQYGGDNY RPFCTEALPL LVRVIQSADS 

       970        980        990       1000       1010       1020 
KTKENVNATE NCISAVGKIM KFKPDCVNVE EVLPHWLSWL PLHEDKEEAV QTFNYLCDLI 

      1030       1040       1050       1060       1070       1080 
ESNHPIVLGP NNTNLPKIFS IIAEGEMHEA IKHEDPCAKR LANVVRQVQT SGGLWTECIA 

      1090 
QLSPEQQAAI QELLNSA 

« Hide

Isoform 2 [UniParc].

Checksum: 7D9A925F7DBC1DE0
Show »

FASTA1,037116,982
Isoform 3 [UniParc].

Checksum: 5296EF23A427A0FB
Show »

FASTA1,115125,545

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. 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] (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. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., 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. 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 (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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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].
[17]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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 ALA-2, 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.
CCDSCCDS31999.1. [O00410-3]
RefSeqNP_002262.3. NM_002271.4. [O00410-3]
XP_005254106.1. XM_005254049.1. [O00410-3]
XP_005254109.1. XM_005254052.1. [O00410-3]
XP_005254110.1. XM_005254053.1. [O00410-3]
UniGeneHs.712598.

3D structure databases

ProteinModelPortalO00410.
SMRO00410. Positions 14-607.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110041. 56 interactions.
DIPDIP-41042N.
IntActO00410. 24 interactions.
MINTMINT-132356.
STRING9606.ENSP00000261574.

PTM databases

PhosphoSiteO00410.

Proteomic databases

MaxQBO00410.
PaxDbO00410.
PRIDEO00410.

Protocols and materials databases

DNASU3843.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261574; ENSP00000261574; ENSG00000065150. [O00410-3]
ENST00000357602; ENSP00000350219; ENSG00000065150. [O00410-1]
ENST00000490680; ENSP00000418393; ENSG00000065150. [O00410-1]
GeneID3843.
KEGGhsa:3843.
UCSCuc001vne.3. human. [O00410-3]
uc001vnf.1. human. [O00410-1]

Organism-specific databases

CTD3843.
GeneCardsGC13P098605.
H-InvDBHIX0174410.
HGNCHGNC:6402. IPO5.
HPACAB009110.
HPA056548.
MIM602008. gene.
neXtProtNX_O00410.
PharmGKBPA30193.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5215.
HOGENOMHOG000209725.
HOVERGENHBG006156.
InParanoidO00410.
OMADTNLNNM.
OrthoDBEOG7Q5HCD.
PhylomeDBO00410.
TreeFamTF300344.

Gene expression databases

ArrayExpressO00410.
BgeeO00410.
CleanExHS_IPO5.
GenevestigatorO00410.

Family and domain databases

Gene3D1.25.10.10. 3 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR001494. Importin-beta_N.
[Graphical view]
PfamPF02985. HEAT. 2 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
PROSITEPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIPO5. human.
GeneWikiRANBP5.
GenomeRNAi3843.
NextBio15125.
PROO00410.
SOURCESearch...

Entry information

Entry nameIPO5_HUMAN
AccessionPrimary (citable) accession number: O00410
Secondary accession number(s): B4DZA0 expand/collapse secondary AC list , O15257, Q5T578, Q86XC7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 141 of the entry and version 4 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 13

Human chromosome 13: entries, gene names and cross-references to MIM