Q9HAV4 (XPO5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Exportin-5
Short name=Exp5

Alternative name(s):
Ran-binding protein 21

Gene names

Name:	XPO5
Synonyms:	KIAA1291, RANBP21

Organism

Homo sapiens (Human) [Complete 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	1204 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	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). Ref.1 Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 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
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. Ref.1 Ref.2 Ref.10 Ref.14
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.

Ontologies

Keywords
Biological process	Protein transport RNA-mediated gene silencing Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	RNA-binding tRNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	gene silencing by RNA Inferred from electronic annotation. Source: UniProtKB-KW protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular function	protein binding Inferred from physical interaction. Source: IntAct tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FADD	Q13158	1	EBI-517949,EBI-494804
GSTK1	Q9Y2Q3	1	EBI-517949,EBI-1053767
MAGEA6	P43360	1	EBI-517949,EBI-1045155
NEK6	Q9HC98	1	EBI-517949,EBI-740364
PHLDA3	Q9Y5J5	1	EBI-517949,EBI-1055859
PTP4A3	O75365	1	EBI-517949,EBI-1043866
SERINC3	Q13530	1	EBI-517949,EBI-1045571

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 1204	1203	Exportin-5		PRO_0000235299
Regions
	Region	2 – 108	107	Necessary for interaction with Ran
	Region	533 – 640	108	Necessary for interaction with ILF3
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.20
	Modified residue	396	1	N6-acetyllysine Ref.21
	Modified residue	826	1	Phosphoserine Ref.18
Natural variations
	Natural variant	241	1	S → N. [dbSNP:rs34324334]		VAR_048960
	Natural variant	610	1	K → N. [dbSNP:rs12173786]		VAR_028032
Experimental info
	Sequence conflict	81	1	G → S in AAG53603. Ref.1
	Sequence conflict	697	1	A → V in BAA86605. Ref.3
	Sequence conflict	988	1	A → T in BAB14200. Ref.5
	Sequence conflict	1151	1	K → E in BAA91547. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9HAV4-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 3295A17DF7C37602	FASTA	1,204	136,311
	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

References

	« Hide 'large scale' referencesShow '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: 12426392] [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: 11777942] [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: 10574462] [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: 12168954] [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. , 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: 14574404] [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: 15489334] [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, 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: 17974005] [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. , 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: 14702039] [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: 12426393] [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: 14681208] [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: 12509441] [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: 14570900] [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: 15254228] [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: 14730017] [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: 14631048] [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: 15613540] [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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, MASS SPECTROMETRY.
+	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.

IPI

IPI00640703.

PIR

T46411.

RefSeq

NP_065801.1.

UniGene

Hs.203206.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3A6P	X-ray	2.92	A/F	1-1204	[»]

ProteinModelPortal

Q9HAV4.

SMR

Q9HAV4. Positions 11-165.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9HAV4. 16 interactions.

MINT

MINT-264827.

STRING

Q9HAV4.

PTM databases

PhosphoSite

Q9HAV4.

Proteomic databases

PRIDE

Q9HAV4.

Genome annotation databases

Ensembl

ENST00000265351; ENSP00000265351; ENSG00000124571; Homo sapiens. [Genome view]

GeneID

57510.

KEGG

hsa:57510.

UCSC

uc003ovp.1. human.

Organism-specific databases

CTD

57510.

GeneCards

GC06M043490.

H-InvDB

HIX0005908.

HGNC

HGNC:17675. XPO5.

HPA

CAB012357.
HPA018402.
HPA023959.
HPA029909.
HPA029910.

MIM

607845. gene.

PharmGKB

PA134979214.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09712.

HOVERGEN

HBG056281.

PhylomeDB

Q9HAV4.

Enzyme and pathway databases

Reactome

REACT_12472. Regulatory RNA pathways.

Gene expression databases

ArrayExpress

Q9HAV4.

Bgee

Q9HAV4.

Genevestigator

Q9HAV4.

GermOnline

ENSG00000124571. Homo sapiens.

Family and domain databases

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013598. Exportin-1/Importin-b-like.
[Graphical view]

Gene3D

G3DSA:1.25.10.10. ARM-like. 1 hit.

Pfam

PF08389. Xpo1. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

63866.

PMAP-CutDB

Q9HAV4.

SOURCE

Search...

Entry information

Entry name

XPO5_HUMAN

Accession

Primary (citable) accession number: Q9HAV4
Secondary accession number(s): Q5JTE6 , 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:	August 10, 2010
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.