CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000735
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Exportin-T 
Protein Synonyms/Alias
 Exportin(tRNA); tRNA exportin 
Gene Name
 XPOT 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
172ARRNTLIKDTMREQCubiquitination[1, 2]
316LIKNGDIKNAQEALQubiquitination[1]
557RFVKSLNKQMNPFIEubiquitination[3, 4]
627LLTPLMEKFKILLEKacetylation[5]
627LLTPLMEKFKILLEKubiquitination[2, 3, 4]
629TPLMEKFKILLEKLMubiquitination[2, 3, 4]
634KFKILLEKLMLAQDEacetylation[5]
634KFKILLEKLMLAQDEubiquitination[2, 3, 4]
950QPDAKVFKNYLKVFFubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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
Functional Description
 Mediates the nuclear export of aminoacylated tRNAs. In the nucleus binds to tRNA 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 tRNA from the export receptor. XPOT 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
 REGION 1 385 Necessary for interaction with Ran,
 REGION 443 962 Necessary for tRNA-binding, cytoplasmic
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 634 634 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Polymorphism; Reference proteome; RNA-binding; Transport; tRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 962 AA 
Protein Sequence
MDEQALLGLN PNADSDFRQR ALAYFEQLKI SPDAWQVCAE ALAQRTYSDD HVKFFCFQVL 60
EHQVKYKYSE LTTVQQQLIR ETLISWLQAQ MLNPQPEKTF IRNKAAQVFA LLFVTEYLTK 120
WPKFFFDILS VVDLNPRGVD LYLRILMAID SELVDRDVVH TSEEARRNTL IKDTMREQCI 180
PNLVESWYQI LQNYQFTNSE VTCQCLEVVG AYVSWIDLSL IANDRFINML LGHMSIEVLR 240
EEACDCLFEV VNKGMDPVDK MKLVESLCQV LQSAGFFSID QEEDVDFLAR FSKLVNGMGQ 300
SLIVSWSKLI KNGDIKNAQE ALQAIETKVA LMLQLLIHED DDISSNIIGF CYDYLHILKQ 360
LTVLSDQQKA NVEAIMLAVM KKLTYDEEYN FENEGEDEAM FVEYRKQLKL LLDRLAQVSP 420
ELLLASVRRV FSSTLQNWQT TRFMEVEVAI RLLYMLAEAL PVSHGAHFSG DVSKASALQD 480
MMRTLVTSGV SSYQHTSVTL EFFETVVRYE KFFTVEPQHI PCVLMAFLDH RGLRHSSAKV 540
RSRTAYLFSR FVKSLNKQMN PFIEDILNRI QDLLELSPPE NGHQSLLSSD DQLFIYETAG 600
VLIVNSEYPA ERKQALMRNL LTPLMEKFKI LLEKLMLAQD EERQASLADC LNHAVGFASR 660
TSKAFSNKQT VKQCGCSEVY LDCLQTFLPA LSCPLQKDIL RSGVRTFLHR MIICLEEEVL 720
PFIPSASEHM LKDCEAKDLQ EFIPLINQIT AKFKIQVSPF LQQMFMPLLH AIFEVLLRPA 780
EENDQSAALE KQMLRRSYFA FLQTVTGSGM SEVIANQGAE NVERVLVTVI QGAVEYPDPI 840
AQKTCFIILS KLVELWGGKD GPVGFADFVY KHIVPACFLA PLKQTFDLAD AQTVLALSEC 900
AVTLKTIHLK RGPECVQYLQ QEYLPSLQVA PEIIQEFCQA LQQPDAKVFK NYLKVFFQRA 960
KP 962 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005643; C:nuclear pore; IEA:InterPro.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0008565; F:protein transporter activity; IEA:InterPro.
 GO:0000049; F:tRNA binding; IDA:UniProtKB.
 GO:0006886; P:intracellular protein transport; IEA:InterPro.
 GO:0006409; P:tRNA export from nucleus; IDA:UniProtKB. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR013598; Exportin-1/Importin-b-like.
 IPR001494; Importin-beta_N. 
Pfam
 PF03810; IBN_N
 PF08389; Xpo1 
SMART
 SM00913; IBN_N 
PROSITE
  
PRINTS