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O15397 (IPO8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 110. 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-8

Short name=Imp8
Alternative name(s):
Ran-binding protein 8
Short name=RanBP8
Gene names
Name:IPO8
Synonyms:RANBP8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1037 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to function 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. In vitro mediates the nuclear import of SRP19. Ref.1 Ref.4

Subunit structure

Forms a heterodimer with KPNB1. Interacts with SRP19. Binds directly to nuclear pore complexes. Ref.1 Ref.4

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the importin beta family.

Contains 1 importin N-terminal domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processintracellular protein transport

Inferred from electronic annotation. Source: InterPro

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRan GTPase binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15397-1)

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: O15397-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-213: MDLNRIIQAL...ILKIFYALVQ → MESLTLK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10371037Importin-8
PRO_0000120752

Regions

Domain22 – 10281Importin N-terminal
Compositional bias923 – 9286Poly-Glu

Amino acid modifications

Modified residue9021Phosphoserine Ref.6 Ref.7 Ref.9
Modified residue9031Phosphoserine Ref.6 Ref.7 Ref.9

Natural variations

Alternative sequence1 – 213213MDLNR…YALVQ → MESLTLK in isoform 2.
VSP_042574
Natural variant61I → F. Ref.1
Corresponds to variant rs1054423 [ dbSNP | Ensembl ].
VAR_055118
Natural variant6401I → V.
Corresponds to variant rs34119940 [ dbSNP | Ensembl ].
VAR_055119

Experimental info

Sequence conflict911Q → R in AAB67052. Ref.1
Sequence conflict2791P → A in AAB67052. Ref.1

Sequences

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

Last modified May 5, 2009. Version 2.
Checksum: 3D7195FD57D7D9AF

FASTA1,037119,938
        10         20         30         40         50         60 
MDLNRIIQAL KGTIDPKLRI AAENELNQSY KIINFAPSLL RIIVSDHVEF PVRQAAAIYL 

        70         80         90        100        110        120 
KNMVTQYWPD REPPPGEAIF PFNIHENDRQ QIRDNIVEGI IRSPDLVRVQ LTMCLRAIIK 

       130        140        150        160        170        180 
HDFPGHWPGV VDKIDYYLQS QSSASWLGSL LCLYQLVKTY EYKKAEEREP LIIAMQIFLP 

       190        200        210        220        230        240 
RIQQQIVQLL PDSSYYSVLL QKQILKIFYA LVQYALPLQL VNNQTMTTWM EIFRTIIDRT 

       250        260        270        280        290        300 
VPPETLHIDE DDRPELVWWK CKKWALHIVA RLFERYGSPG NVTKEYFEFS EFFLKTYAVG 

       310        320        330        340        350        360 
IQQVLLKILD QYRQKEYVAP RVLQQAFNYL NQGVVHSITW KQMKPHIQNI SEDVIFSVMC 

       370        380        390        400        410        420 
YKDEDEELWQ EDPYEYIRMK FDIFEDYASP TTAAQTLLYT AAKKRKEVLP KMMAFCYQIL 

       430        440        450        460        470        480 
TDPNFDPRKK DGALHVIGSL AEILLKKSLF KDQMELFLQN HVFPLLLSNL GYLRARSCWV 

       490        500        510        520        530        540 
LHAFSSLKFH NELNLRNAVE LAKKSLIEDK EMPVKVEAAL ALQSLISNQI QAKEYMKPHV 

       550        560        570        580        590        600 
RPIMQELLHI VRETENDDVT NVIQKMICEY SQEVASIAVD MTQHLAEIFG KVLQSDEYEE 

       610        620        630        640        650        660 
VEDKTVMAMG ILHTIDTILT VVEDHKEITQ QLENICLRII DLVLQKHVIE FYEEILSLAY 

       670        680        690        700        710        720 
SLTCHSISPQ MWQLLGILYE VFQQDCFEYF TDMMPLLHNY VTIDTDTLLS NAKHLEILFT 

       730        740        750        760        770        780 
MCRKVLCGDA GEDAECHAAK LLEVIILQCK GRGIDQCIPL FVQLVLERLT RGVKTSELRT 

       790        800        810        820        830        840 
MCLQVAIAAL YYNPDLLLHT LERIQLPHNP GPITVQFINQ WMNDTDCFLG HHDRKMCIIG 

       850        860        870        880        890        900 
LSILLELQNR PPAVDAVVGQ IVPSILFLFL GLKQVCATRQ LVNREDRSKA EKADMEENEE 

       910        920        930        940        950        960 
ISSDEEETNV TAQAMQSNNG RGEDEEEEDD DWDEEVLEET ALEGFSTPLD LDNSVDEYQF 

       970        980        990       1000       1010       1020 
FTQALITVQS RDAAWYQLLM APLSEDQRTA LQEVYTLAEH RRTVAEAKKK IEQQGGFTFE 

      1030 
NKGVLSAFNF GTVPSNN 

« Hide

Isoform 2 [UniParc].

Checksum: 80607ACB36848EEB
Show »

FASTA83195,979

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH KPNB1, VARIANT PHE-6.
[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] (ISOFORM 2).
Tissue: Testis.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Signal recognition particle protein 19 is imported into the nucleus by importin 8 (RanBP8) and transportin."
Dean K.A., von Ahsen O., Goerlich D., Fried H.M.
J. Cell Sci. 114:3479-3485(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SRP19.
[5]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"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-902 AND SER-903, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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-902 AND SER-903, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"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].
[9]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902 AND SER-903, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U77494 mRNA. Translation: AAB67052.1.
AK302260 mRNA. Translation: BAH13659.1.
AC012673 Genomic DNA. No translation available.
AC023426 Genomic DNA. No translation available.
RefSeqNP_001177924.1. NM_001190995.1.
NP_006381.2. NM_006390.3.
UniGeneHs.505136.

3D structure databases

ProteinModelPortalO15397.
SMRO15397. Positions 96-159, 388-444, 509-553, 738-769.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115781. 14 interactions.
IntActO15397. 10 interactions.
MINTMINT-1150774.
STRING9606.ENSP00000256079.

PTM databases

PhosphoSiteO15397.

Proteomic databases

PaxDbO15397.
PRIDEO15397.

Protocols and materials databases

DNASU10526.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256079; ENSP00000256079; ENSG00000133704. [O15397-1]
ENST00000544829; ENSP00000444520; ENSG00000133704.
GeneID10526.
KEGGhsa:10526.
UCSCuc001rjd.3. human. [O15397-1]
uc001rje.1. human. [O15397-2]

Organism-specific databases

CTD10526.
GeneCardsGC12M030682.
HGNCHGNC:9853. IPO8.
HPAHPA018439.
HPA023765.
MIM605600. gene.
neXtProtNX_O15397.
PharmGKBPA34214.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5656.
HOGENOMHOG000006586.
HOVERGENHBG006824.
InParanoidO15397.
OMAIQAKEYM.
OrthoDBEOG7TF787.
PhylomeDBO15397.
TreeFamTF300634.

Gene expression databases

ArrayExpressO15397.
BgeeO15397.
CleanExHS_IPO8.
GenevestigatorO15397.

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. 1 hit.
PROSITEPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi10526.
NextBio39934.
PROO15397.
SOURCESearch...

Entry information

Entry nameIPO8_HUMAN
AccessionPrimary (citable) accession number: O15397
Secondary accession number(s): B7Z7M3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 5, 2009
Last modified: March 19, 2014
This is version 110 of the entry and version 2 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 12

Human chromosome 12: entries, gene names and cross-references to MIM