UniProt Accession

 XPO2_HUMAN; P55060; A3RLL6; B2R5T4; E1P5Y0; F8W904; O75432; Q32M40; Q9H5B7; Q9NTS0; Q9UP98; Q9UP99; Q9UPA0 

Genbank Protein ID

 U33286; AF053640; AF053641; AF053642; AF053651; AF053644; AF053645; AF053646; AF053647; AF053648; AF053649; AF053650; EF426455; AK312306; AL121903; AL133174; AL133174; AL121903; CH471077; CH471077; BC108309; BC109313; BC109314 

Genbank Nucleotide ID

 AAC50367.1; AAC35007.1; AAC35008.1; AAC35009.1; AAC35297.1; AAC35297.1; AAC35297.1; AAC35297.1; AAC35297.1; AAC35297.1; AAC35297.1; AAC35297.1; ABO15009.1; BAG35231.1; CAI19615.1; CAI19615.1; CAI42818.1; CAI42818.1; EAW75676.1; EAW75677.1; AAI08310.1; AAI09314.1; AAI09315.1 

Protein Name

 Exportin-2 

Protein Synonyms/Alias

 Exp2; Cellular apoptosis susceptibility protein; Chromosome segregation 1-like protein; Importin-alpha re-exporter 

Gene Name

 CSE1L 

Gene Synonyms/Alias

 CAS; XPO2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
17	TLTEYLKKTLDPDPA	ubiquitination	[1]
126	GREDFPQKWPDLLTE	ubiquitination	[2]
158	RTAHSLFKRYRHEFK	acetylation	[1, 3, 4]
165	KRYRHEFKSNELWTE	ubiquitination	[5, 6, 7]
346	TLTSICEKVIVPNME	ubiquitination	[8]
440	LVTSLASKAQTQKHG	ubiquitination	[2, 5, 6, 7]
481	VNEFPVLKADGIKYI	ubiquitination	[2]
574	SENEYIMKAIMRSFS	acetylation	[3]
726	IASAAADKIPGLLGV	ubiquitination	[5, 7]
824	MFGMVLEKIIIPEIQ	acetylation	[3]
824	MFGMVLEKIIIPEIQ	ubiquitination	[5, 7]
848	ICAVGITKLLTECPP	ubiquitination	[9]
925	GQMVNNPKIHLAQSL	ubiquitination	[5, 7]
934	HLAQSLHKLSTACPG	ubiquitination	[5, 6, 7, 10]

Reference

 [1] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [10] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 29 102 Importin N-terminal.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 574 574 N6-acetyllysine.
 MOD_RES 824 824 N6-acetyllysine.  

Keyword

 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Polymorphism; Protein transport; Reference proteome; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 971 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO:0005643; C:nuclear pore; IEA:InterPro.
 GO:0005634; C:nucleus; TAS:ProtInc.
 GO:0008262; F:importin-alpha export receptor activity; TAS:ProtInc.
 GO:0006915; P:apoptotic process; TAS:ProtInc.
 GO:0008283; P:cell proliferation; TAS:ProtInc. 

Interpro

 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR005043; CAS_CSE1_C.
 IPR013713; Exportin/Importin_Cse1-like.
 IPR001494; Importin-beta_N. 

Pfam

 PF03378; CAS_CSE1
 PF08506; Cse1
 PF03810; IBN_N 

SMART

 SM00913; IBN_N 

PROSITE

 PS50166; IMPORTIN_B_NT 

PRINTS