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P55060 (XPO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exportin-2

Short name=Exp2
Alternative name(s):
Cellular apoptosis susceptibility protein
Chromosome segregation 1-like protein
Importin-alpha re-exporter
Gene names
Name:CSE1L
Synonyms:CAS, XPO2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length971 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Export receptor for importin-alpha. Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates (cargos) have been released into the nucleoplasm. In the nucleus binds cooperatively to importin-alpha 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 importin-alpha from the export receptor. CSE1L/XPO2 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. Ref.9

Subunit structure

Found in a complex with CSE1L/XPO2, Ran and KPNA2. Binds with high affinity to importin-alpha only in the presence of RanGTP. The complex is dissociated by the combined action of RanBP1 and RanGAP1. Ref.9

Subcellular location

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

Tissue specificity

Highly expressed in proliferating cells.

Sequence similarities

Belongs to the XPO2/CSE1 family.

Contains 1 importin N-terminal domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TP53P046375EBI-286709,EBI-366083

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P55060-1)

Also known as: A;

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: P55060-2)

The sequence of this isoform differs from the canonical sequence as follows:
     190-195: ATIELC → VWNASW
     196-971: Missing.
Isoform 3 (identifier: P55060-3)

The sequence of this isoform differs from the canonical sequence as follows:
     943-945: VPS → TYF
     946-971: Missing.
Isoform 4 (identifier: P55060-4)

The sequence of this isoform differs from the canonical sequence as follows:
     257-312: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 971971Exportin-2
PRO_0000117287

Regions

Domain29 – 10274Importin N-terminal

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8 Ref.11 Ref.14 Ref.15
Modified residue5741N6-acetyllysine Ref.12
Modified residue8241N6-acetyllysine Ref.12

Natural variations

Alternative sequence190 – 1956ATIELC → VWNASW in isoform 2.
VSP_001222
Alternative sequence196 – 971776Missing in isoform 2.
VSP_001223
Alternative sequence257 – 31256Missing in isoform 4.
VSP_047203
Alternative sequence943 – 9453VPS → TYF in isoform 3.
VSP_001224
Alternative sequence946 – 97126Missing in isoform 3.
VSP_001225
Natural variant7541I → V.
Corresponds to variant rs2229042 [ dbSNP | Ensembl ].
VAR_029327
Natural variant8421C → F in a colorectal cancer sample; somatic mutation. Ref.16
VAR_036558
Natural variant9681V → L.
Corresponds to variant rs3505 [ dbSNP | Ensembl ].
VAR_048836

Experimental info

Sequence conflict231 – 2333FED → WEG in AAC50367. Ref.1
Sequence conflict231 – 2333FED → WEG in AAC35008. Ref.2
Sequence conflict5141E → G in AAC50367. Ref.1
Sequence conflict5141E → G in AAC35008. Ref.2
Sequence conflict5381A → T in ABO15009. Ref.3
Sequence conflict8481K → N in AAC50367. Ref.1
Sequence conflict9341K → M in AAC50367. Ref.1

Sequences

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

Last modified March 29, 2005. Version 3.
Checksum: 08E837AB5008EBFD

FASTA971110,417
        10         20         30         40         50         60 
MELSDANLQT LTEYLKKTLD PDPAIRRPAE KFLESVEGNQ NYPLLLLTLL EKSQDNVIKV 

        70         80         90        100        110        120 
CASVTFKNYI KRNWRIVEDE PNKICEADRV AIKANIVHLM LSSPEQIQKQ LSDAISIIGR 

       130        140        150        160        170        180 
EDFPQKWPDL LTEMVNRFQS GDFHVINGVL RTAHSLFKRY RHEFKSNELW TEIKLVLDAF 

       190        200        210        220        230        240 
ALPLTNLFKA TIELCSTHAN DASALRILFS SLILISKLFY SLNFQDLPEF FEDNMETWMN 

       250        260        270        280        290        300 
NFHTLLTLDN KLLQTDDEEE AGLLELLKSQ ICDNAALYAQ KYDEEFQRYL PRFVTAIWNL 

       310        320        330        340        350        360 
LVTTGQEVKY DLLVSNAIQF LASVCERPHY KNLFEDQNTL TSICEKVIVP NMEFRAADEE 

       370        380        390        400        410        420 
AFEDNSEEYI RRDLEGSDID TRRRAACDLV RGLCKFFEGP VTGIFSGYVN SMLQEYAKNP 

       430        440        450        460        470        480 
SVNWKHKDAA IYLVTSLASK AQTQKHGITQ ANELVNLTEF FVNHILPDLK SANVNEFPVL 

       490        500        510        520        530        540 
KADGIKYIMI FRNQVPKEHL LVSIPLLINH LQAESIVVHT YAAHALERLF TMRGPNNATL 

       550        560        570        580        590        600 
FTAAEIAPFV EILLTNLFKA LTLPGSSENE YIMKAIMRSF SLLQEAIIPY IPTLITQLTQ 

       610        620        630        640        650        660 
KLLAVSKNPS KPHFNHYMFE AICLSIRITC KANPAAVVNF EEALFLVFTE ILQNDVQEFI 

       670        680        690        700        710        720 
PYVFQVMSLL LETHKNDIPS SYMALFPHLL QPVLWERTGN IPALVRLLQA FLERGSNTIA 

       730        740        750        760        770        780 
SAAADKIPGL LGVFQKLIAS KANDHQGFYL LNSIIEHMPP ESVDQYRKQI FILLFQRLQN 

       790        800        810        820        830        840 
SKTTKFIKSF LVFINLYCIK YGALALQEIF DGIQPKMFGM VLEKIIIPEI QKVSGNVEKK 

       850        860        870        880        890        900 
ICAVGITKLL TECPPMMDTE YTKLWTPLLQ SLIGLFELPE DDTIPDEEHF IDIEDTPGYQ 

       910        920        930        940        950        960 
TAFSQLAFAG KKEHDPVGQM VNNPKIHLAQ SLHKLSTACP GRVPSMVSTS LNAEALQYLQ 

       970 
GYLQAASVTL L 

« Hide

Isoform 2 [UniParc].

Checksum: 94798963277F26F5
Show »

FASTA19522,670
Isoform 3 [UniParc].

Checksum: 6E2D39436F2ABDD9
Show »

FASTA945107,778
Isoform 4 [UniParc].

Checksum: 6EDE8048022CF7D1
Show »

FASTA915103,879

References

« Hide 'large scale' references
[1]"Cloning and characterization of a cellular apoptosis susceptibility gene, the human homologue to the yeast chromosome segregation gene CSE1."
Brinkmann U., Brinkmann E., Gallo M., Pastan I.
Proc. Natl. Acad. Sci. U.S.A. 92:10427-10431(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"Tissue-specific alternative splicing of the CSE1L/CAS (cellular apoptosis susceptibility) gene."
Brinkmann U., Brinkmann E., Bera T.K., Wellmann A., Pastan I.
Genomics 58:41-49(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
Tissue: Brain.
[3]"IRF-1-mediated CAS expression enhances interferon-gamma-induced apoptosis of HT-29 colon adenocarcinoma cells."
Jiang M.C., Lin T.L., Lee T.L., Huang H.T., Lin C.L., Liao C.F.
Mol. Cell Biol. Res. Commun. 4:353-358(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[4]"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 1).
Tissue: Cerebellum.
[5]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM 1).
Tissue: Testis.
[8]Bienvenut W.V.
Submitted (JUN-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-16; 18-26; 32-67; 76-83; 94-109; 138-151; 166-217; 252-268; 282-288; 293-309; 332-371; 373-382; 396-418; 428-440; 446-481; 560-574; 698-736; 769-777; 789-816; 825-832 AND 913-934, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[9]"Export of importin-alpha from the nucleus is mediated by a specific nuclear transport factor."
Kutay U., Bischoff F.R., Kostka S., Kraft R., Goerlich D.
Cell 90:1061-1071(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 356-370, FUNCTION IN PROTEIN NUCLEAR EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN AND KPNA2.
[10]"Determination of the functional domain organization of the importin alpha nuclear import factor."
Herold A., Truant R., Wiegand H., Cullen B.R.
J. Cell Biol. 143:309-318(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KPNA2.
[11]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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-574 AND LYS-824, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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].
[14]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-842.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U33286 mRNA. Translation: AAC50367.1.
AF053640 mRNA. Translation: AAC35007.1.
AF053641 mRNA. Translation: AAC35008.1.
AF053642 mRNA. Translation: AAC35009.1.
AF053651 expand/collapse EMBL AC list , AF053644, AF053645, AF053646, AF053647, AF053648, AF053649, AF053650 Genomic DNA. Translation: AAC35297.1.
EF426455 mRNA. Translation: ABO15009.1.
AK312306 mRNA. Translation: BAG35231.1.
AL121903, AL133174 Genomic DNA. Translation: CAI19615.1.
AL133174, AL121903 Genomic DNA. Translation: CAI42818.1.
CH471077 Genomic DNA. Translation: EAW75676.1.
CH471077 Genomic DNA. Translation: EAW75677.1.
BC108309 mRNA. Translation: AAI08310.1.
BC109313 mRNA. Translation: AAI09314.1.
BC109314 mRNA. Translation: AAI09315.1.
PIRI39166.
RefSeqNP_001243064.1. NM_001256135.1.
NP_001307.2. NM_001316.3.
UniGeneHs.90073.

3D structure databases

ProteinModelPortalP55060.
SMRP55060. Positions 6-934.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107821. 77 interactions.
DIPDIP-32573N.
IntActP55060. 25 interactions.
MINTMINT-5001090.

PTM databases

PhosphoSiteP55060.

Polymorphism databases

DMDM62297557.

Proteomic databases

PaxDbP55060.
PRIDEP55060.

Protocols and materials databases

DNASU1434.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262982; ENSP00000262982; ENSG00000124207. [P55060-1]
ENST00000396192; ENSP00000379495; ENSG00000124207. [P55060-4]
GeneID1434.
KEGGhsa:1434.
UCSCuc002xty.4. human. [P55060-1]
uc010zyh.3. human. [P55060-3]

Organism-specific databases

CTD1434.
GeneCardsGC20P047662.
HGNCHGNC:2431. CSE1L.
HPACAB002140.
HPA038059.
MIM601342. gene.
neXtProtNX_P55060.
PharmGKBPA26933.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5657.
HOVERGENHBG080050.
InParanoidP55060.
OMAQFVTAVW.
OrthoDBEOG76MK7M.
PhylomeDBP55060.
TreeFamTF300473.

Gene expression databases

ArrayExpressP55060.
BgeeP55060.
CleanExHS_CSE1L.
GenevestigatorP55060.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR005043. CAS_CSE1_C.
IPR013713. Cse1.
IPR001494. Importin-beta_N.
[Graphical view]
PfamPF03378. CAS_CSE1. 1 hit.
PF08506. 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

ChiTaRSCSE1L. human.
GenomeRNAi1434.
NextBio5853.
PROP55060.
SOURCESearch...

Entry information

Entry nameXPO2_HUMAN
AccessionPrimary (citable) accession number: P55060
Secondary accession number(s): A3RLL6 expand/collapse secondary AC list , B2R5T4, E1P5Y0, F8W904, O75432, Q32M40, Q9H5B7, Q9NTS0, Q9UP98, Q9UP99, Q9UPA0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 29, 2005
Last modified: April 16, 2014
This is version 133 of the entry and version 3 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 20

Human chromosome 20: entries, gene names and cross-references to MIM