XPO4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: XPO4_MOUSE
• UniProt AC: Q9ESJ0
• Protein Name: Exportin-4
• Gene Name: Xpo4
• Organism: Mus musculus (Mouse).
• Sequence Length: 1151
• Subcellular Localization: Cytoplasm. Nucleus. Shuttles between the nucleus and the cytoplasm..
• Protein Description: 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 (By similarity)..
• Protein Sequence: MMAAALGPPEVIAQLENAAKVLMAPPSMVSNEQRQHAEHIFLSFRKSKSPFAVCRHILETSKVDYVLFQAATAIMEAVVREWVLLEKGSIESLRTFLLTYVLQRPNLQKYVREQILLAVAVIVKRGSLDKSIDCKSIFHEVSQLISSGNPTVQTLACSILTALLSEFSSSSKTSNIGLSMEFHGNCKRVFQEEDLRQIFMLTVGVLQEFSRRENLSAQMSSVFQRYLALANQVLSWNFLPPKLGRHYIAMFESSQNVLLKPTESWREALLDSRVMELFFTVHRKIREDSDMAQDSLQCLAQLASLHGPIFPDEGSQVDYLAHFIEGLLNTINGIEIEDSEAVGISSIISNLITVFPRNVLTAIPSELFSSFVNCLTHLTCSFGRSAALEEVLDKDDMVYMEAYDKLLESWLTLVRDDKHFHKGFFTQHAVQVFNSYIQCHLAAPDGTRNLTANGVASREEEEISELQEDDRDQFSDQLASVGMLGRIAAEHCMPLLTSLLEERVTRLHGQLQRHQQQFLASPGSSTIDNKMLDDLYEDIHWLILVTGYLLADDTQGETPLIPPEIMEYSIKHSSEVDINTTLQILGSPGEKASSIPGYSRTDSVIRLLSAVLRVSEVESRAIRADLTHLLSPQMGKDIVWFLKRWAKTYLLVDEKLYDQISLPLSTAFGADTEGSQWIIGYLLQKVISNLSVWSSEQDLANDTVQLLVTLVERRERANLVIQCENWWNLAKQFASRSPPLNFLSSPVQRTLMKALVLGGFAHMDTETKQQYWTEVLQPLQQRFLRVINQENFQQMCQQEEVKQEITATLEALCGIAEATQIDNVAILFNFLMDFLNNCIGLMEVYKNTPETVNLIIEVFVEVAHKQICYLGESKAMHLYEACLTLLQVYSKNNLGRQRIDVTAEEEQYQDLLLIMELLTNLLSKEFIDFSDTDEVFRGHEPGQAAGRSVSAADVVLYGVNLILPLMSQDLLKFPTLCNQYYKLITFICEIFPEKIPQLPEDLFKSLMYSLELGMTSMSSEVCQLCLEALTPLAEQCAKAQETDSPLFLATRHFLKLVFDMLVLQKHNTEMTTAAGEAFYTLVCLHQAEYSELVETLLSSQQDPVIYQRLADAFNKLTASSTPPALDRKQKMAFLKSLEEFMANVGGLLCVK

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
95	Phosphorylation	GSIESLRTFLLTYVL CCHHHHHHHHHHHHH	24.75	21454597
99	Phosphorylation	SLRTFLLTYVLQRPN HHHHHHHHHHHHCCC	17.46	21454597
110	Phosphorylation	QRPNLQKYVREQILL HCCCHHHHHHHHHHH	7.56	21454597
210	Phosphorylation	VGVLQEFSRRENLSA HHHHHHHHHHCCHHH	29.67	29233185
216	Phosphorylation	FSRRENLSAQMSSVF HHHHCCHHHHHHHHH	28.21	29895711
464	Phosphorylation	SREEEEISELQEDDR CCCHHHHHHHCCCCH	35.22	21149613
521	Phosphorylation	HQQQFLASPGSSTID HHHHHHCCCCCCHHC	31.76	27087446
524	Phosphorylation	QFLASPGSSTIDNKM HHHCCCCCCHHCCHH	27.91	25168779
525	Phosphorylation	FLASPGSSTIDNKML HHCCCCCCHHCCHHH	34.98	25619855
526	Phosphorylation	LASPGSSTIDNKMLD HCCCCCCHHCCHHHH	33.76	25619855
594	Phosphorylation	SPGEKASSIPGYSRT CCCCCCCCCCCCCCH	37.35	22807455
737	Phosphorylation	AKQFASRSPPLNFLS HHHHHHCCCCCCCCC	28.51	20531401

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

Oops, there are no upstream regulatory protein records of XPO4_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of XPO4_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 XPO4_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of XPO4_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASSSPECTROMETRY.
PubMed: 19367708