dbPTM

XPO5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	XPO5_HUMAN
UniProt AC	Q9HAV4
Protein Name	Exportin-5
Gene Name	XPO5
Organism	Homo sapiens (Human).
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). Mediates nuclear export of isoform 5 of ADAR/ADAR1 in a RanGTP-dependent manner.; Mediates the nuclear export of micro-RNA precursors, which form short hairpins. [PubMed: 14681208]
Protein Sequence	MAMDQVNALCEQLVKAVTVMMDPNSTQRYRLEALKFCEEFKEKCPICVPCGLRLAEKTQVAIVRHFGLQILEHVVKFRWNGMSRLEKVYLKNSVMELIANGTLNILEEENHIKDALSRIVVEMIKREWPQHWPDMLIELDTLSKQGETQTELVMFILLRLAEDVVTFQTLPPQRRRDIQQTLTQNMERIFSFLLNTLQENVNKYQQVKTDTSQESKAQANCRVGVAALNTLAGYIDWVSMSHITAENCKLLEILCLLLNEQELQLGAAECLLIAVSRKGKLEDRKPLMVLFGDVAMHYILSAAQTADGGGLVEKHYVFLKRLCQVLCALGNQLCALLGADSDVETPSNFGKYLESFLAFTTHPSQFLRSSTQMTWGALFRHEILSRDPLLLAIIPKYLRASMTNLVKMGFPSKTDSPSCEYSRFDFDSDEDFNAFFNSSRAQQGEVMRLACRLDPKTSFQMAGEWLKYQLSTFLDAGSVNSCSAVGTGEGSLCSVFSPSFVQWEAMTLFLESVITQMFRTLNREEIPVNDGIELLQMVLNFDTKDPLILSCVLTNVSALFPFVTYRPEFLPQVFSKLFSSVTFETVEESKAPRTRAVRNVRRHACSSIIKMCRDYPQLVLPNFDMLYNHVKQLLSNELLLTQMEKCALMEALVLISNQFKNYERQKVFLEELMAPVASIWLSQDMHRVLSDVDAFIAYVGTDQKSCDPGLEDPCGLNRARMSFCVYSILGVVKRTCWPTDLEEAKAGGFVVGYTSSGNPIFRNPCTEQILKLLDNLLALIRTHNTLYAPEMLAKMAEPFTKALDMLDAEKSAILGLPQPLLELNDSPVFKTVLERMQRFFSTLYENCFHILGKAGPSMQQDFYTVEDLATQLLSSAFVNLNNIPDYRLRPMLRVFVKPLVLFCPPEHYEALVSPILGPLFTYLHMRLSQKWQVINQRSLLCGEDEAADENPESQEMLEEQLVRMLTREVMDLITVCCVSKKGADHSSAPPADGDDEEMMATEVTPSAMAELTDLGKCLMKHEDVCTALLITAFNSLAWKDTLSCQRTTSQLCWPLLKQVLSGTLLADAVTWLFTSVLKGLQMHGQHDGCMASLVHLAFQIYEALRPRYLEIRAVMEQIPEIQKDSLDQFDCKLLNPSLQKVADKRRKDQFKRLIAGCIGKPLGEQFRKEVHIKNLPSLFKKTKPMLETEVLDNDGGGLATIFEP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAMDQVNAL ------CCHHHHHHH	22.89	22223895
18	Phosphorylation	EQLVKAVTVMMDPNS HHHHHHHHHHCCCCC	13.93	21406692
20	Sulfoxidation	LVKAVTVMMDPNSTQ HHHHHHHHCCCCCCH	1.52	21406390
25	Phosphorylation	TVMMDPNSTQRYRLE HHHCCCCCCHHHHHH	31.16	21406692
26	Phosphorylation	VMMDPNSTQRYRLEA HHCCCCCCHHHHHHH	24.57	21406692
35	Ubiquitination	RYRLEALKFCEEFKE HHHHHHHHHHHHHHH	55.82	32015554
41	Acetylation	LKFCEEFKEKCPICV HHHHHHHHHHCCEEC	60.59	25953088
41	Ubiquitination	LKFCEEFKEKCPICV HHHHHHHHHHCCEEC	60.59	29967540
43	Ubiquitination	FCEEFKEKCPICVPC HHHHHHHHCCEECCC	45.99	-
83	Phosphorylation	KFRWNGMSRLEKVYL HHCCCCCCHHHHHHH	34.80	28509920
123	Sulfoxidation	LSRIVVEMIKREWPQ HHHHHHHHHHHHCCC	2.71	21406390
125	Ubiquitination	RIVVEMIKREWPQHW HHHHHHHHHHCCCCC	42.85	-
169	Phosphorylation	EDVVTFQTLPPQRRR HCCCCCCCCCHHHHH	36.72	-
208	Ubiquitination	VNKYQQVKTDTSQES HHHHHHCCCCCCHHH	36.02	21906983
208 (in isoform 1)	Ubiquitination	-	36.02	21890473
216	Ubiquitination	TDTSQESKAQANCRV CCCCHHHHHHHHHHH	43.71	-
278	Ubiquitination	LLIAVSRKGKLEDRK HHHHHHCCCCCCCCC	53.55	24816145
369	Phosphorylation	HPSQFLRSSTQMTWG CHHHHHHHCCCCCHH	39.63	-
374	Phosphorylation	LRSSTQMTWGALFRH HHHCCCCCHHHHHHH	15.78	-
385	Phosphorylation	LFRHEILSRDPLLLA HHHHHHHCCCHHHHH	40.06	24719451
396 (in isoform 1)	Ubiquitination	-	46.65	21890473
396	Acetylation	LLLAIIPKYLRASMT HHHHHHHHHHHHHHH	46.65	19608861
396	Ubiquitination	LLLAIIPKYLRASMT HHHHHHHHHHHHHHH	46.65	23000965
397	Phosphorylation	LLAIIPKYLRASMTN HHHHHHHHHHHHHHH	8.96	28270605
401	Phosphorylation	IPKYLRASMTNLVKM HHHHHHHHHHHHHHC	21.50	24719451
403	Phosphorylation	KYLRASMTNLVKMGF HHHHHHHHHHHHCCC	23.94	24719451
412	Phosphorylation	LVKMGFPSKTDSPSC HHHCCCCCCCCCCCC	46.02	23312004
413	Ubiquitination	VKMGFPSKTDSPSCE HHCCCCCCCCCCCCC	57.50	21963094
414	Phosphorylation	KMGFPSKTDSPSCEY HCCCCCCCCCCCCCC	46.15	27732954
416	Phosphorylation	GFPSKTDSPSCEYSR CCCCCCCCCCCCCCC	24.76	25159151
418	Phosphorylation	PSKTDSPSCEYSRFD CCCCCCCCCCCCCCC	24.43	27732954
421	Phosphorylation	TDSPSCEYSRFDFDS CCCCCCCCCCCCCCC	14.96	23312004
422	Phosphorylation	DSPSCEYSRFDFDSD CCCCCCCCCCCCCCC	12.27	27794612
428	Phosphorylation	YSRFDFDSDEDFNAF CCCCCCCCCHHHHHH	42.78	22617229
448	Methylation	AQQGEVMRLACRLDP HCCCCHHHHHHCCCC	25.06	-
497	Phosphorylation	GSLCSVFSPSFVQWE CCCCCCCCCCHHHHH	19.92	-
590	Ubiquitination	FETVEESKAPRTRAV CCCHHHCCCCCHHHH	66.73	-
606	Phosphorylation	NVRRHACSSIIKMCR HHHHHHHHHHHHHHC	25.92	21406692
607	Phosphorylation	VRRHACSSIIKMCRD HHHHHHHHHHHHHCC	28.37	21406692
610	Ubiquitination	HACSSIIKMCRDYPQ HHHHHHHHHHCCCCC	30.22	23000965
610	Acetylation	HACSSIIKMCRDYPQ HHHHHHHHHHCCCCC	30.22	25953088
662	Phosphorylation	ISNQFKNYERQKVFL HHHHCCCHHHHHHHH	17.06	-
704	Ubiquitination	AYVGTDQKSCDPGLE HHHCCCCCCCCCCCC	56.73	21963094
722	Phosphorylation	GLNRARMSFCVYSIL CCCHHHHHHHHHHHH	15.22	20068231
726	Phosphorylation	ARMSFCVYSILGVVK HHHHHHHHHHHHHHH	7.38	20068231
727	Phosphorylation	RMSFCVYSILGVVKR HHHHHHHHHHHHHHH	7.31	20068231
753	Phosphorylation	AGGFVVGYTSSGNPI CCCEEEEECCCCCCC	7.58	19276368
755	Phosphorylation	GFVVGYTSSGNPIFR CEEEEECCCCCCCCC	27.97	19276368
756	Phosphorylation	FVVGYTSSGNPIFRN EEEEECCCCCCCCCC	34.49	19276368
782	Phosphorylation	NLLALIRTHNTLYAP HHHHHHHHCCCCCCH	16.69	20071362
785	Phosphorylation	ALIRTHNTLYAPEML HHHHHCCCCCCHHHH	17.34	20071362
787	Phosphorylation	IRTHNTLYAPEMLAK HHHCCCCCCHHHHHH	20.33	20071362
791	Sulfoxidation	NTLYAPEMLAKMAEP CCCCCHHHHHHHHHH	4.25	28183972
800	Phosphorylation	AKMAEPFTKALDMLD HHHHHHHHHHHHHHH	26.56	-
801 (in isoform 1)	Ubiquitination	-	47.53	21890473
801	Ubiquitination	KMAEPFTKALDMLDA HHHHHHHHHHHHHHH	47.53	21906983
810	Acetylation	LDMLDAEKSAILGLP HHHHHHHHHHHHCCC	47.08	7407677
810	Ubiquitination	LDMLDAEKSAILGLP HHHHHHHHHHHHCCC	47.08	29967540
826	Phosphorylation	PLLELNDSPVFKTVL HHHHCCCCHHHHHHH	23.14	22617229
922	Phosphorylation	ILGPLFTYLHMRLSQ HHHHHHHHHHHHHHH	6.30	-
930	Ubiquitination	LHMRLSQKWQVINQR HHHHHHHHHHHHCCH	35.90	21890473
930 (in isoform 1)	Ubiquitination	-	35.90	21890473
941	Glutathionylation	INQRSLLCGEDEAAD HCCHHHHCCCCHHCC	7.32	22555962
981	Ubiquitination	TVCCVSKKGADHSSA HHHHCCCCCCCCCCC	52.40	-
1123	Acetylation	EQIPEIQKDSLDQFD HHCCHHCCCCCCHHC	55.75	26051181
1125	Phosphorylation	IPEIQKDSLDQFDCK CCHHCCCCCCHHCHH	40.66	28674419
1132	Acetylation	SLDQFDCKLLNPSLQ CCCHHCHHHHCHHHH	58.83	23236377
1132	Ubiquitination	SLDQFDCKLLNPSLQ CCCHHCHHHHCHHHH	58.83	32015554
1137	Phosphorylation	DCKLLNPSLQKVADK CHHHHCHHHHHHHHH	42.21	20068231
1140	Ubiquitination	LLNPSLQKVADKRRK HHCHHHHHHHHHHCH	44.69	21890473
1140 (in isoform 1)	Ubiquitination	-	44.69	21890473
1140	Acetylation	LLNPSLQKVADKRRK HHCHHHHHHHHHHCH	44.69	25953088
1160 (in isoform 1)	Ubiquitination	-	19.70	21890473
1160	Acetylation	LIAGCIGKPLGEQFR HHHHHHCCHHHHHHH	19.70	26051181
1160	Ubiquitination	LIAGCIGKPLGEQFR HHHHHHCCHHHHHHH	19.70	29967540
1173	Malonylation	FRKEVHIKNLPSLFK HHHHHHHHCHHHHHH	37.24	26320211
1173	Ubiquitination	FRKEVHIKNLPSLFK HHHHHHHHCHHHHHH	37.24	32015554
1173 (in isoform 1)	Ubiquitination	-	37.24	21890473
1177	Phosphorylation	VHIKNLPSLFKKTKP HHHHCHHHHHHHCCC	49.99	24719451
1180 (in isoform 1)	Ubiquitination	-	65.90	21890473
1180	Acetylation	KNLPSLFKKTKPMLE HCHHHHHHHCCCCEE	65.90	25953088
1180	Ubiquitination	KNLPSLFKKTKPMLE HCHHHHHHHCCCCEE	65.90	21890473
1181	Ubiquitination	NLPSLFKKTKPMLET CHHHHHHHCCCCEEE	55.22	-
1182	Phosphorylation	LPSLFKKTKPMLETE HHHHHHHCCCCEEEE	40.76	-
1183	Ubiquitination	PSLFKKTKPMLETEV HHHHHHCCCCEEEEE	36.99	-

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of XPO5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of XPO5_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of XPO5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EF1A1_HUMAN	EEF1A1	physical	12426393
RAN_HUMAN	RAN	physical	11777942
NU214_HUMAN	NUP214	physical	11777942
NU153_HUMAN	NUP153	physical	11777942
AASD1_HUMAN	AARSD1	physical	22863883
U5S1_HUMAN	EFTUD2	physical	22863883
RNZ2_HUMAN	ELAC2	physical	22863883
SYHC_HUMAN	HARS	physical	22863883
P3H1_HUMAN	P3H1	physical	22863883
MAT2B_HUMAN	MAT2B	physical	22863883
NRDC_HUMAN	NRD1	physical	22863883
NSUN2_HUMAN	NSUN2	physical	22863883
PDIA6_HUMAN	PDIA6	physical	22863883
PFD5_HUMAN	PFDN5	physical	22863883
MYPT1_HUMAN	PPP1R12A	physical	22863883
SYSC_HUMAN	SARS	physical	22863883
GDN_HUMAN	SERPINE2	physical	22863883
GLYC_HUMAN	SHMT1	physical	22863883
SNX5_HUMAN	SNX5	physical	22863883
TTC1_HUMAN	TTC1	physical	22863883
UGDH_HUMAN	UGDH	physical	22863883
NUP98_HUMAN	NUP98	physical	26344197
PPME1_HUMAN	PPME1	physical	26344197
STOM_HUMAN	STOM	physical	27173435

Drug and Disease Associations

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

Regulatory Network of XPO5_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826, AND MASSSPECTROMETRY.	18691976 [Abstract]