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Protein

Exportin-4

Gene

XPO4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO4 then return to the nuclear compartment and 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.2 Publications

GO - Biological processi

  1. positive regulation of protein export from nucleus Source: BHF-UCL
  2. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Exportin-4
Short name:
Exp4
Gene namesi
Name:XPO4
Synonyms:KIAA1721
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:17796. XPO4.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Shuttles between the nucleus and the cytoplasm.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134866468.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11511151Exportin-4PRO_0000204711Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei464 – 4641Phosphoserine2 Publications
Modified residuei521 – 5211Phosphoserine5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9C0E2.
PaxDbiQ9C0E2.
PRIDEiQ9C0E2.

PTM databases

PhosphoSiteiQ9C0E2.

Expressioni

Gene expression databases

BgeeiQ9C0E2.
CleanExiHS_XPO4.
ExpressionAtlasiQ9C0E2. baseline and differential.
GenevestigatoriQ9C0E2.

Interactioni

Subunit structurei

Found in a complex with XPO4, Ran and EIF5A. Found in a complex with XPO4, Ran and SMAD3. Interacts with SMAD3. Interacts with Ran and cargo proteins in a GTP-dependent manner.2 Publications

Protein-protein interaction databases

BioGridi122138. 29 interactions.
IntActiQ9C0E2. 1 interaction.
STRINGi9606.ENSP00000255305.

Structurei

3D structure databases

ProteinModelPortaliQ9C0E2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the exportin family.Curated

Phylogenomic databases

eggNOGiNOG273883.
GeneTreeiENSGT00730000111055.
HOGENOMiHOG000154878.
HOVERGENiHBG023214.
InParanoidiQ9C0E2.
OrthoDBiEOG7FJGZW.
PhylomeDBiQ9C0E2.
TreeFamiTF312991.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014877. CRM1_C_dom.
[Graphical view]
PfamiPF08767. CRM1_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 5 hits.

Sequencei

Sequence statusi: Complete.

Q9C0E2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMAAALGPPE VIAQLENAAK VLMAPPSMVN NEQRQHAEHI FLSFRKSKSP
60 70 80 90 100
FAVCKHILET SKVDYVLFQA ATAIMEAVVR EWILLEKGSI ESLRTFLLTY
110 120 130 140 150
VLQRPNLQKY VREQILLAVA VIVKRGSLDK SIDCKSIFHE VSQLISSGNP
160 170 180 190 200
TVQTLACSIL TALLSEFSSS SKTSNIGLSM EFHGNCKRVF QEEDLRQIFM
210 220 230 240 250
LTVEVLQEFS RRENLNAQMS SVFQRYLALA NQVLSWNFLP PNLGRHYIAM
260 270 280 290 300
FESSQNVLLK PTESWRETLL DSRVMELFFT VHRKIREDSD MAQDSLQCLA
310 320 330 340 350
QLASLHGPIF PDEGSQVDYL AHFIEGLLNT INGIEIEDSE AVGISSIISN
360 370 380 390 400
LITVFPRNVL TAIPSELFSS FVNCLTHLTC SFGRSAALEE VLDKDDMVYM
410 420 430 440 450
EAYDKLLESW LTLVQDDKHF HKGFFTQHAV QVFNSYIQCH LAAPDGTRNL
460 470 480 490 500
TANGVASREE EEISELQEDD RDQFSDQLAS VGMLGRIAAE HCIPLLTSLL
510 520 530 540 550
EERVTRLHGQ LQRHQQQLLA SPGSSTVDNK MLDDLYEDIH WLILVTGYLL
560 570 580 590 600
ADDTQGETPL IPPEIMEYSI KHSSEVDINT TLQILGSPGE KASSIPGYNR
610 620 630 640 650
TDSVIRLLSA ILRVSEVESR AIRADLTHLL SPQMGKDIVW FLKRWAKTYL
660 670 680 690 700
LVDEKLYDQI SLPFSTAFGA DTEGSQWIIG YLLQKVISNL SVWSSEQDLA
710 720 730 740 750
NDTVQLLVTL VERRERANLV IQCENWWNLA KQFASRSPPL NFLSSPVQRT
760 770 780 790 800
LMKALVLGGF AHMDTETKQQ YWTEVLQPLQ QRFLRVINQE NFQQMCQQEE
810 820 830 840 850
VKQEITATLE ALCGIAEATQ IDNVAILFNF LMDFLTNCIG LMEVYKNTPE
860 870 880 890 900
TVNLIIEVFV EVAHKQICYL GESKAMNLYE ACLTLLQVYS KNNLGRQRID
910 920 930 940 950
VTAEEEQYQD LLLIMELLTN LLSKEFIDFS DTDEVFRGHE PGQAANRSVS
960 970 980 990 1000
AADVVLYGVN LILPLMSQDL LKFPTLCNQY YKLITFICEI FPEKIPQLPE
1010 1020 1030 1040 1050
DLFKSLMYSL ELGMTSMSSE VCQLCLEALT PLAEQCAKAQ ETDSPLFLAT
1060 1070 1080 1090 1100
RHFLKLVFDM LVLQKHNTEM TTAAGEAFYT LVCLHQAEYS ELVETLLSSQ
1110 1120 1130 1140 1150
QDPVIYQRLA DAFNKLTASS TPPTLDRKQK MAFLKSLEEF MANVGGLLCV

K
Length:1,151
Mass (Da):130,139
Last modified:November 1, 2001 - v2
Checksum:i38E7EEFC938B07C5
GO

Sequence cautioni

The sequence BAB14409.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti511 – 5111L → S in BAB14409 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti149 – 1491N → S.
Corresponds to variant rs17320607 [ dbSNP | Ensembl ].
VAR_048958
Natural varianti451 – 4511T → A.
Corresponds to variant rs9552285 [ dbSNP | Ensembl ].
VAR_048959

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051508 mRNA. Translation: BAB21812.1.
AL512652, AL356285 Genomic DNA. Translation: CAH71795.1.
AL356285, AL512652 Genomic DNA. Translation: CAI15862.1.
AK023108 mRNA. Translation: BAB14409.1. Different initiation.
AL831819 mRNA. Translation: CAD38533.2.
CCDSiCCDS41872.1.
RefSeqiNP_071904.4. NM_022459.4.
UniGeneiHs.507452.

Genome annotation databases

EnsembliENST00000255305; ENSP00000255305; ENSG00000132953.
GeneIDi64328.
KEGGihsa:64328.
UCSCiuc001unq.4. human.

Polymorphism databases

DMDMi17368720.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051508 mRNA. Translation: BAB21812.1.
AL512652, AL356285 Genomic DNA. Translation: CAH71795.1.
AL356285, AL512652 Genomic DNA. Translation: CAI15862.1.
AK023108 mRNA. Translation: BAB14409.1. Different initiation.
AL831819 mRNA. Translation: CAD38533.2.
CCDSiCCDS41872.1.
RefSeqiNP_071904.4. NM_022459.4.
UniGeneiHs.507452.

3D structure databases

ProteinModelPortaliQ9C0E2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122138. 29 interactions.
IntActiQ9C0E2. 1 interaction.
STRINGi9606.ENSP00000255305.

PTM databases

PhosphoSiteiQ9C0E2.

Polymorphism databases

DMDMi17368720.

Proteomic databases

MaxQBiQ9C0E2.
PaxDbiQ9C0E2.
PRIDEiQ9C0E2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000255305; ENSP00000255305; ENSG00000132953.
GeneIDi64328.
KEGGihsa:64328.
UCSCiuc001unq.4. human.

Organism-specific databases

CTDi64328.
GeneCardsiGC13M021351.
H-InvDBHIX0011162.
HGNCiHGNC:17796. XPO4.
MIMi611449. gene.
neXtProtiNX_Q9C0E2.
PharmGKBiPA134866468.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG273883.
GeneTreeiENSGT00730000111055.
HOGENOMiHOG000154878.
HOVERGENiHBG023214.
InParanoidiQ9C0E2.
OrthoDBiEOG7FJGZW.
PhylomeDBiQ9C0E2.
TreeFamiTF312991.

Miscellaneous databases

GeneWikiiXPO4.
GenomeRNAii64328.
NextBioi66257.
PROiQ9C0E2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9C0E2.
CleanExiHS_XPO4.
ExpressionAtlasiQ9C0E2. baseline and differential.
GenevestigatoriQ9C0E2.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014877. CRM1_C_dom.
[Graphical view]
PfamiPF08767. CRM1_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 5 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1151.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 888-1151.
    Tissue: Skeletal muscle.
  5. "Exportin 4: a mediator of a novel nuclear export pathway in higher eukaryotes."
    Lipowsky G., Bischoff F.R., Schwarzmaier P., Kraft R., Kostka S., Hartmann E., Kutay U., Goerlich D.
    EMBO J. 19:4362-4371(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION IN NUCLEAR PROTEIN EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN AND EIF5A.
  6. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "The mechanism of nuclear export of Smad3 involves exportin 4 and Ran."
    Kurisaki A., Kurisaki K., Kowanetz M., Sugino H., Yoneda Y., Heldin C.-H., Moustakas A.
    Mol. Cell. Biol. 26:1318-1332(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NUCLEAR PROTEIN EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN AND SMAD3, INTERACTION WITH SMAD3, SUBCELLULAR LOCATION.
  8. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464 AND SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiXPO4_HUMAN
AccessioniPrimary (citable) accession number: Q9C0E2
Secondary accession number(s): Q5VUZ5, Q8N3V6, Q9H934
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2001
Last sequence update: November 1, 2001
Last modified: March 3, 2015
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.