XPO5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: XPO5_MOUSE
• UniProt AC: Q924C1
• Protein Name: Exportin-5
• Gene Name: Xpo5
• Organism: Mus musculus (Mouse).
• Sequence Length: 1204
• Subcellular Localization: Nucleus . Cytoplasm . Shuttles between the nucleus and the cytoplasm.
• Protein Description: 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) (By similarity). Mediates nuclear export of ADAR/ADAR1 in a RanGTP-dependent manner (By similarity).; 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. 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 (By similarity)..
• Protein Sequence: MEMEQVNALCEELVKAVTVMMDPSSTQRYRLEALKFCEEFKEKCPICVPCGLKLAEKTQIAIVRHFGLQILEHVVKFRWNSMSRLEKVYLKNSVMELIANGTLRILEEENHIKDVLSRIVVEMIKREWPQHWPDMLMELDTLFRQGETQRELVMFILLRLAEDVVTFQTLPTQRRRDIQQTLTQNMERILNFLLNTLQENVNKYQQMKTDSSQEAEAQANCRVSVAALNTLAGYIDWVSLNHITAENCKLVETLCLLLNEQELQLGAAECLLIAVSRKGKLEDRKRLMILFGDVAMHYILSAAQTADGGGLVEKHYLFLKRLCQVLCALGNLLCALLALDANIQTPINFGMYLESFLAFTTHPSQFLRSSTHMTWGALFRHEVLSRDPALLAVIPKYLRASMTNLVKMGFPSKTDSPSCEYSRFDFDSDEDFNAFFNSSRAQHGEVVRCVCRLDPKTSFQMAAEWLKYQLSASIDTGPVNSCSTAGTGEGGFCSIFSPSYVQWEAMTFFLESVINQMFRTLDKEELPVSDGIELLQLVLNFEIKDPLVLSCVLTNVSALFPFVTYKPAFLPQVFSKLFSFVTFESVGESKAPRTRAVRNVRRHACSSINKMCRDYPDLVLPNFDMLYSHVKQLLSNELLLTQMEKCALMEALVLVSNQFKDYERQKLFLEELMAPVVNIWLSEEMCRALSDIDSFIAYVGADLKSCDPAVEDPCGLNRARMSFCVYSILGVMRRTSWPSDLEEAKAGGFVVGYTPSGNPIFRNPCTEQILRLLDNLLALVRTHNTLYTPEMLTKMAEPFTKALDIVESEKTAILGLPQPLLEFNDHPVYRTTLERMQRFFGILYENCYHILGKAGPSMQQDFYTVEDLASQLLGSAFVNLNNIPDFRLRSMLRVFVKPLVLFCPSEHYETLISPILGPLFTYLHMRLSQKWHVINQRSILCGEDEIAEDNPESQEMLEEQLVRMLTREAMDLIMACCVSKKTADHTAAPTADGDDEEMMATEVAPSSVVELTDLGKCLMKHEDVCTALLITAFNSLTWKDTLSCQRATTQLCWPLLKQVMSGTLLADAVTWLFTSVLKGLQMHGQHDGCMASLVHLAFQIYEALRPRYLEIRAVMEQIPEINKESLDQFDCKLLNPSLQKAADKRRKDHFKRLIAGCIGKPLGEQFRKEVHIKNLPWLFKKPKPMLETEVLDSEEGGLATIFEP

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
41	Ubiquitination	LKFCEEFKEKCPICV HHHHHHHHHHCCEEC	60.59	-
211	Phosphorylation	YQQMKTDSSQEAEAQ HHHHCCCCHHHHHHH	38.87	21082442
212	Phosphorylation	QQMKTDSSQEAEAQA HHHCCCCHHHHHHHH	34.55	21082442
320	Acetylation	EKHYLFLKRLCQVLC HHHHHHHHHHHHHHH	35.67	2415579
396	Acetylation	ALLAVIPKYLRASMT HHHHHHHHHHHHHHH	45.88	-
396	Ubiquitination	ALLAVIPKYLRASMT HHHHHHHHHHHHHHH	45.88	-
407	Ubiquitination	ASMTNLVKMGFPSKT HHHHHHHHCCCCCCC	36.15	-
413	Ubiquitination	VKMGFPSKTDSPSCE HHCCCCCCCCCCCCC	57.50	-
416	Phosphorylation	GFPSKTDSPSCEYSR CCCCCCCCCCCCCCC	24.76	29514104
590	Ubiquitination	FESVGESKAPRTRAV HHCCCCCCCCHHHHH	59.10	-
610	Ubiquitination	HACSSINKMCRDYPD HHHHHHHHHHHCCCC	37.39	-
735	Phosphorylation	ILGVMRRTSWPSDLE HHHHHHHCCCCCCHH	25.44	28066266
736	Phosphorylation	LGVMRRTSWPSDLEE HHHHHHCCCCCCHHH	34.87	28066266
739	Phosphorylation	MRRTSWPSDLEEAKA HHHCCCCCCHHHHHC	48.87	28066266
966	Phosphorylation	EQLVRMLTREAMDLI HHHHHHHHHHHHHHH	19.68	-
979	Phosphorylation	LIMACCVSKKTADHT HHHHHHCCCCCCCCC	17.96	-
1137	Phosphorylation	DCKLLNPSLQKAADK CHHHHCHHHHHHHHH	42.21	27841257
1160	Acetylation	LIAGCIGKPLGEQFR HHHHHHCCHHHHHHH	19.70	22826441

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of XPO5_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of XPO5_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of XPO5_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of XPO5_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.