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Q9HAV4 (XPO5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Exportin-5

Short name=Exp5
Alternative name(s):
Ran-binding protein 21
Gene names
Name:XPO5
Synonyms:KIAA1291, RANBP21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates the nuclear export of proteins bearing a double-stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase Ran in its active GTP-bound form. Proteins containing dsRBDs can associate with this trimeric complex through the RNA. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause disassembly of the complex and release of the cargo from the export receptor. XPO5 then returns to the nuclear compartment by diffusion through the nuclear pore complex, to mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Overexpression may in some circumstances enhance RNA-mediated gene silencing (RNAi). Mediates nuclear export of isoform 5of ADAR/ADAR1 in a RanGTP-dependent manner. Ref.1 Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.20

Mediates the nuclear export of micro-RNA precursors, which form short hairpins. Also mediates the nuclear export of synthetic short hairpin RNAs used for RNA interference, and adenovirus VA1 dsRNA. In some circumstances can also mediate the nuclear export of deacylated and aminoacylated tRNAs. Specifically recognizes dsRNAs that lack a 5'-overhang in a sequence-independent manner, have only a short 3'-overhang, and that have a double-stranded length of at least 15 base-pairs. Binding is dependent on Ran-GTP. Ref.1 Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.20

Subunit structure

Component of a nuclear export receptor complex composed of XPO5, Ran, dsRNA-binding proteins and dsRNA. Found in a nuclear export complex with XPO5, Ran, EEF1A1, and aminoacylated tRNA. Found in a nuclear export complex with XPO5, Ran, ILF3 and dsRNA. Found in a nuclear export complex with XPO5, Ran and pre-miRNA. Found in a nuclear export complex with XPO5, Ran, ILF3 and minihelix VA1 dsRNA. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and dsRNA. Interacts with EEF1A1, ILF3, NUP153, NUP214 and ZNF346. Interacts with Ran and cargo proteins in a GTP-dependent manner. Interacts with isoform 5of ADAR/ADAR1 (via DRBM domains). Ref.1 Ref.2 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16 Ref.20

Subcellular location

Nucleus. Cytoplasm. Note: Shuttles between the nucleus and the cytoplasm. Ref.2

Tissue specificity

Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas. Ref.2

Sequence similarities

Belongs to the exportin family.

Sequence caution

The sequence AAH00129.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA86605.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAA91547.1 differs from that shown. Reason: Frameshift at position 920.

The sequence CAI42640.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.19
Chain2 – 12041203Exportin-5
PRO_0000235299

Regions

Region2 – 108107Necessary for interaction with Ran
Region533 – 640108Necessary for interaction with ILF3

Amino acid modifications

Modified residue21N-acetylalanine Ref.19 Ref.23
Modified residue3961N6-acetyllysine Ref.21
Modified residue8261Phosphoserine Ref.18

Natural variations

Natural variant2411S → N.
Corresponds to variant rs34324334 [ dbSNP | Ensembl ].
VAR_048960
Natural variant6101K → N.
Corresponds to variant rs12173786 [ dbSNP | Ensembl ].
VAR_028032

Experimental info

Sequence conflict811G → S in AAG53603. Ref.1
Sequence conflict6971A → V in BAA86605. Ref.3
Sequence conflict9881A → T in BAB14200. Ref.5
Sequence conflict11511K → E in BAA91547. Ref.5

Secondary structure

............................................................................................................................................. 1204
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HAV4 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 3295A17DF7C37602

FASTA1,204136,311
        10         20         30         40         50         60 
MAMDQVNALC EQLVKAVTVM MDPNSTQRYR LEALKFCEEF KEKCPICVPC GLRLAEKTQV 

        70         80         90        100        110        120 
AIVRHFGLQI LEHVVKFRWN GMSRLEKVYL KNSVMELIAN GTLNILEEEN HIKDALSRIV 

       130        140        150        160        170        180 
VEMIKREWPQ HWPDMLIELD TLSKQGETQT ELVMFILLRL AEDVVTFQTL PPQRRRDIQQ 

       190        200        210        220        230        240 
TLTQNMERIF SFLLNTLQEN VNKYQQVKTD TSQESKAQAN CRVGVAALNT LAGYIDWVSM 

       250        260        270        280        290        300 
SHITAENCKL LEILCLLLNE QELQLGAAEC LLIAVSRKGK LEDRKPLMVL FGDVAMHYIL 

       310        320        330        340        350        360 
SAAQTADGGG LVEKHYVFLK RLCQVLCALG NQLCALLGAD SDVETPSNFG KYLESFLAFT 

       370        380        390        400        410        420 
THPSQFLRSS TQMTWGALFR HEILSRDPLL LAIIPKYLRA SMTNLVKMGF PSKTDSPSCE 

       430        440        450        460        470        480 
YSRFDFDSDE DFNAFFNSSR AQQGEVMRLA CRLDPKTSFQ MAGEWLKYQL STFLDAGSVN 

       490        500        510        520        530        540 
SCSAVGTGEG SLCSVFSPSF VQWEAMTLFL ESVITQMFRT LNREEIPVND GIELLQMVLN 

       550        560        570        580        590        600 
FDTKDPLILS CVLTNVSALF PFVTYRPEFL PQVFSKLFSS VTFETVEESK APRTRAVRNV 

       610        620        630        640        650        660 
RRHACSSIIK MCRDYPQLVL PNFDMLYNHV KQLLSNELLL TQMEKCALME ALVLISNQFK 

       670        680        690        700        710        720 
NYERQKVFLE ELMAPVASIW LSQDMHRVLS DVDAFIAYVG TDQKSCDPGL EDPCGLNRAR 

       730        740        750        760        770        780 
MSFCVYSILG VVKRTCWPTD LEEAKAGGFV VGYTSSGNPI FRNPCTEQIL KLLDNLLALI 

       790        800        810        820        830        840 
RTHNTLYAPE MLAKMAEPFT KALDMLDAEK SAILGLPQPL LELNDSPVFK TVLERMQRFF 

       850        860        870        880        890        900 
STLYENCFHI LGKAGPSMQQ DFYTVEDLAT QLLSSAFVNL NNIPDYRLRP MLRVFVKPLV 

       910        920        930        940        950        960 
LFCPPEHYEA LVSPILGPLF TYLHMRLSQK WQVINQRSLL CGEDEAADEN PESQEMLEEQ 

       970        980        990       1000       1010       1020 
LVRMLTREVM DLITVCCVSK KGADHSSAPP ADGDDEEMMA TEVTPSAMAE LTDLGKCLMK 

      1030       1040       1050       1060       1070       1080 
HEDVCTALLI TAFNSLAWKD TLSCQRTTSQ LCWPLLKQVL SGTLLADAVT WLFTSVLKGL 

      1090       1100       1110       1120       1130       1140 
QMHGQHDGCM ASLVHLAFQI YEALRPRYLE IRAVMEQIPE IQKDSLDQFD CKLLNPSLQK 

      1150       1160       1170       1180       1190       1200 
VADKRRKDQF KRLIAGCIGK PLGEQFRKEV HIKNLPSLFK KTKPMLETEV LDNDGGGLAT 


IFEP 

« Hide

References

« Hide 'large scale' references
[1]"Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm."
Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E., Hartmann E., Goerlich D.
EMBO J. 21:6205-6215(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PROTEIN AND TRNA NUCLEAR EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH EEF1A1; RAN AND TRNA, INTERACTION WITH EEF1A1, RNA-BINDING.
[2]"Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins."
Brownawell A.M., Macara I.G.
J. Cell Biol. 156:53-64(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PROTEIN NUCLEAR EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH ILF3; RAN AND DOUBLE-STRANDED RNA, INTERACTION WITH ILF3; NUP153 AND NUP214, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Brain.
[3]"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
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].
Tissue: Ascites, Placenta, Retinoblastoma and Rhabdomyosarcoma.
[7]Bienvenut W.V.
Submitted (JUN-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 189-203 AND 387-396, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[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 450-1204.
Tissue: Testis.
[9]"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] OF 537-1204.
Tissue: Teratocarcinoma.
[10]"Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA."
Calado A., Treichel N., Mueller E.-C., Otto A., Kutay U.
EMBO J. 21:6216-6224(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PROTEIN AND TRNA NUCLEAR EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH EEF1A1; RAN AND TRNA, INTERACTION WITH EEF1A1, IDENTIFICATION BY MASS SPECTROMETRY, RNA-BINDING.
[11]"Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RNAs."
Yi R., Qin Y., Macara I.G., Cullen B.R.
Genes Dev. 17:3011-3016(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PRE-MIRNA EXPORT, RNA-BINDING.
[12]"Exportin-5 mediates nuclear export of minihelix-containing RNAs."
Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Doglio A., Bertrand E., Macara I.G., Dargemont C.
J. Biol. Chem. 278:5505-5508(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ADENOVIRUS VA1 RNA EXPORT, RNA-BINDING.
[13]"Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3."
Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Evers S., Macara I.G., Dargemont C.
J. Biol. Chem. 279:884-891(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PROTEIN AND ADENOVIRUS VA1 RNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH ILF3; RAN AND VA1 RNA, RNA-BINDING.
[14]"Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-5."
Chen T., Brownawell A.M., Macara I.G.
Mol. Cell. Biol. 24:6608-6619(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PROTEIN AND DOUBLE-STRANDED RNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH RAN; ILF3; ZNF346 AND DOUBLE-STRANDED RNA, INTERACTION WITH ILF3 AND ZNF346.
[15]"Exportin 5 is a RanGTP-dependent dsRNA-binding protein that mediates nuclear export of pre-miRNAs."
Bohnsack M.T., Czaplinski K., Goerlich D.
RNA 10:185-191(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PRE-MIRNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH RAN AND PRE-MIRNA, RNA-BINDING.
[16]"Nuclear export of microRNA precursors."
Lund E., Guettinger S., Calado A., Dahlberg J.E., Kutay U.
Science 303:95-98(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PRE-MIRNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH RAN AND PRE-MIRNA, RNA-BINDING.
[17]"Overexpression of exportin 5 enhances RNA interference mediated by short hairpin RNAs and microRNAs."
Yi R., Doehle B.P., Qin Y., Macara I.G., Cullen B.R.
RNA 11:220-226(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PRE-MIRNA EXPORT.
[18]"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-826, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[20]"RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1."
Fritz J., Strehblow A., Taschner A., Schopoff S., Pasierbek P., Jantsch M.F.
Mol. Cell. Biol. 29:1487-1497(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ADAR.
[21]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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].
[23]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF271159 mRNA. Translation: AAG53603.1.
AF298880 mRNA. Translation: AAG17907.1.
AB033117 mRNA. Translation: BAA86605.2. Different initiation.
AL355802 Genomic DNA. Translation: CAI42640.1. Sequence problems.
BC000129 mRNA. Translation: AAH00129.1. Different initiation.
BC008347 mRNA. Translation: AAH08347.1.
BC009969 mRNA. Translation: AAH09969.2.
BC062635 mRNA. Translation: AAH62635.1.
AL137467 mRNA. Translation: CAB70753.1.
AK001195 mRNA. Translation: BAA91547.1. Frameshift.
AK022718 mRNA. Translation: BAB14200.1.
CCDSCCDS47430.1.
PIRT46411.
RefSeqNP_065801.1. NM_020750.2.
UniGeneHs.203206.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3A6PX-ray2.92A/F1-1204[»]
ProteinModelPortalQ9HAV4.
SMRQ9HAV4. Positions 58-243.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121574. 54 interactions.
DIPDIP-34547N.
IntActQ9HAV4. 13 interactions.
MINTMINT-264827.

PTM databases

PhosphoSiteQ9HAV4.

Polymorphism databases

DMDM74734245.

Proteomic databases

MaxQBQ9HAV4.
PaxDbQ9HAV4.
PRIDEQ9HAV4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265351; ENSP00000265351; ENSG00000124571.
GeneID57510.
KEGGhsa:57510.
UCSCuc003ovp.3. human.

Organism-specific databases

CTD57510.
GeneCardsGC06M043490.
H-InvDBHIX0005908.
HGNCHGNC:17675. XPO5.
HPACAB012357.
HPA018402.
HPA023959.
HPA029909.
HPA029910.
MIM607845. gene.
neXtProtNX_Q9HAV4.
PharmGKBPA134979214.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG296759.
HOVERGENHBG056281.
KOK14289.
OMAFADSVGH.
OrthoDBEOG7MWGW1.
PhylomeDBQ9HAV4.
TreeFamTF323382.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9HAV4.
BgeeQ9HAV4.
GenevestigatorQ9HAV4.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013598. Exportin-1/Importin-b-like.
IPR001494. Importin-beta_N.
[Graphical view]
PfamPF08389. Xpo1. 1 hit.
[Graphical view]
SMARTSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 4 hits.
ProtoNetSearch...

Other

ChiTaRSXPO5. human.
EvolutionaryTraceQ9HAV4.
GeneWikiXPO5.
GenomeRNAi57510.
NextBio63866.
PMAP-CutDBQ9HAV4.
PROQ9HAV4.
SOURCESearch...

Entry information

Entry nameXPO5_HUMAN
AccessionPrimary (citable) accession number: Q9HAV4
Secondary accession number(s): Q5JTE6 expand/collapse secondary AC list , Q96G48, Q96HN3, Q9BWM6, Q9BZV5, Q9H9M4, Q9NT89, Q9NW39, Q9ULC9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 105 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 6

Human chromosome 6: entries, gene names and cross-references to MIM