dbPTM

XPO2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	XPO2_HUMAN
UniProt AC	P55060
Protein Name	Exportin-2
Gene Name	CSE1L
Organism	Homo sapiens (Human).
Sequence Length	971
Subcellular Localization	Cytoplasm . Nucleus . Shuttles between the nucleus and the cytoplasm.
Protein 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..
Protein Sequence	MELSDANLQTLTEYLKKTLDPDPAIRRPAEKFLESVEGNQNYPLLLLTLLEKSQDNVIKVCASVTFKNYIKRNWRIVEDEPNKICEADRVAIKANIVHLMLSSPEQIQKQLSDAISIIGREDFPQKWPDLLTEMVNRFQSGDFHVINGVLRTAHSLFKRYRHEFKSNELWTEIKLVLDAFALPLTNLFKATIELCSTHANDASALRILFSSLILISKLFYSLNFQDLPEFFEDNMETWMNNFHTLLTLDNKLLQTDDEEEAGLLELLKSQICDNAALYAQKYDEEFQRYLPRFVTAIWNLLVTTGQEVKYDLLVSNAIQFLASVCERPHYKNLFEDQNTLTSICEKVIVPNMEFRAADEEAFEDNSEEYIRRDLEGSDIDTRRRAACDLVRGLCKFFEGPVTGIFSGYVNSMLQEYAKNPSVNWKHKDAAIYLVTSLASKAQTQKHGITQANELVNLTEFFVNHILPDLKSANVNEFPVLKADGIKYIMIFRNQVPKEHLLVSIPLLINHLQAESIVVHTYAAHALERLFTMRGPNNATLFTAAEIAPFVEILLTNLFKALTLPGSSENEYIMKAIMRSFSLLQEAIIPYIPTLITQLTQKLLAVSKNPSKPHFNHYMFEAICLSIRITCKANPAAVVNFEEALFLVFTEILQNDVQEFIPYVFQVMSLLLETHKNDIPSSYMALFPHLLQPVLWERTGNIPALVRLLQAFLERGSNTIASAAADKIPGLLGVFQKLIASKANDHQGFYLLNSIIEHMPPESVDQYRKQIFILLFQRLQNSKTTKFIKSFLVFINLYCIKYGALALQEIFDGIQPKMFGMVLEKIIIPEIQKVSGNVEKKICAVGITKLLTECPPMMDTEYTKLWTPLLQSLIGLFELPEDDTIPDEEHFIDIEDTPGYQTAFSQLAFAGKKEHDPVGQMVNNPKIHLAQSLHKLSTACPGRVPSMVSTSLNAEALQYLQGYLQAASVTLL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MELSDANL -------CCCCHHHH	12.03	22223895
1	Sulfoxidation	-------MELSDANL -------CCCCHHHH	12.03	28183972
4	Phosphorylation	----MELSDANLQTL ----CCCCHHHHHHH	22.75	23401153
10	Phosphorylation	LSDANLQTLTEYLKK CCHHHHHHHHHHHHH	38.52	23401153
12	Phosphorylation	DANLQTLTEYLKKTL HHHHHHHHHHHHHHC	26.43	20068231
14	Phosphorylation	NLQTLTEYLKKTLDP HHHHHHHHHHHHCCC	20.70	23401153
16	Ubiquitination	QTLTEYLKKTLDPDP HHHHHHHHHHCCCCH	42.69	-
17	Acetylation	TLTEYLKKTLDPDPA HHHHHHHHHCCCCHH	52.29	23954790
17	Ubiquitination	TLTEYLKKTLDPDPA HHHHHHHHHCCCCHH	52.29	-
18	Phosphorylation	LTEYLKKTLDPDPAI HHHHHHHHCCCCHHH	34.50	20068231
31	Ubiquitination	AIRRPAEKFLESVEG HHCCCHHHHHHHCCC	58.31	-
52	Ubiquitination	LLLTLLEKSQDNVIK HHHHHHHHCCCCHHH	54.08	-
67	Ubiquitination	VCASVTFKNYIKRNW HHHHHHHHHHHHHCE	39.20	-
67	Acetylation	VCASVTFKNYIKRNW HHHHHHHHHHHHHCE	39.20	25038526
71	Ubiquitination	VTFKNYIKRNWRIVE HHHHHHHHHCEEEEC	29.35	-
83	Acetylation	IVEDEPNKICEADRV EECCCCCCCCHHHHH	60.49	25953088
85	Glutathionylation	EDEPNKICEADRVAI CCCCCCCCHHHHHHH	3.63	22555962
89	Methylation	NKICEADRVAIKANI CCCCHHHHHHHHHHH	27.15	-
100	Sulfoxidation	KANIVHLMLSSPEQI HHHHHHHHCCCHHHH	1.74	28183972
102	Phosphorylation	NIVHLMLSSPEQIQK HHHHHHCCCHHHHHH	29.86	25627689
103	Phosphorylation	IVHLMLSSPEQIQKQ HHHHHCCCHHHHHHH	28.61	25627689
109	Acetylation	SSPEQIQKQLSDAIS CCHHHHHHHHHHHHH	55.63	26051181
112	Phosphorylation	EQIQKQLSDAISIIG HHHHHHHHHHHHHHC	23.62	23917254
116	Phosphorylation	KQLSDAISIIGREDF HHHHHHHHHHCCCCC	15.18	20873877
126	Ubiquitination	GREDFPQKWPDLLTE CCCCCCCCCHHHHHH	62.01	-
132	Phosphorylation	QKWPDLLTEMVNRFQ CCCHHHHHHHHHHHH	29.36	26503514
155	Phosphorylation	GVLRTAHSLFKRYRH HHHHHHHHHHHHHHH	32.79	24719451
158	Acetylation	RTAHSLFKRYRHEFK HHHHHHHHHHHHHHH	54.54	23749302
158	Ubiquitination	RTAHSLFKRYRHEFK HHHHHHHHHHHHHHH	54.54	19608861
165	Ubiquitination	KRYRHEFKSNELWTE HHHHHHHHCCHHHHH	49.76	21890473
165	Ubiquitination	KRYRHEFKSNELWTE HHHHHHHHCCHHHHH	49.76	21890473
165	Acetylation	KRYRHEFKSNELWTE HHHHHHHHCCHHHHH	49.76	27452117
165 (in isoform 1)	Ubiquitination	-	49.76	21890473
165 (in isoform 2)	Ubiquitination	-	49.76	21890473
165 (in isoform 3)	Ubiquitination	-	49.76	21890473
166	Phosphorylation	RYRHEFKSNELWTEI HHHHHHHCCHHHHHH	40.64	21712546
185	Phosphorylation	DAFALPLTNLFKATI HHHHHHHHHHHHHHH	28.12	-
191	Phosphorylation	LTNLFKATIELCSTH HHHHHHHHHHHHHCC	18.64	-
211	Phosphorylation	ALRILFSSLILISKL HHHHHHHHHHHHHHH	16.46	20860994
216	Phosphorylation	FSSLILISKLFYSLN HHHHHHHHHHHHHCC	21.62	20860994
255	Phosphorylation	LDNKLLQTDDEEEAG HCCCCCCCCCHHHHH	45.44	-
268	Ubiquitination	AGLLELLKSQICDNA HHHHHHHHHCCCCCH	53.60	-
269	Phosphorylation	GLLELLKSQICDNAA HHHHHHHHCCCCCHH	25.42	21712546
278	Phosphorylation	ICDNAALYAQKYDEE CCCCHHHHHHHCHHH	11.40	28102081
341	Phosphorylation	FEDQNTLTSICEKVI CCCCCHHHHHHHHHH	17.63	21712546
342	Phosphorylation	EDQNTLTSICEKVIV CCCCHHHHHHHHHHC	28.49	25849741
344	S-nitrosocysteine	QNTLTSICEKVIVPN CCHHHHHHHHHHCCC	4.08	-
344	Glutathionylation	QNTLTSICEKVIVPN CCHHHHHHHHHHCCC	4.08	22555962
344	S-nitrosylation	QNTLTSICEKVIVPN CCHHHHHHHHHHCCC	4.08	19483679
346	Ubiquitination	TLTSICEKVIVPNME HHHHHHHHHHCCCCC	32.61	22053931
346 (in isoform 1)	Ubiquitination	-	32.61	21890473
352	Sulfoxidation	EKVIVPNMEFRAADE HHHHCCCCCEECCCH	4.16	30846556
355	Methylation	IVPNMEFRAADEEAF HCCCCCEECCCHHHH	18.63	-
366	Phosphorylation	EEAFEDNSEEYIRRD HHHHCCCCHHHHHHH	44.09	21815630
369	Phosphorylation	FEDNSEEYIRRDLEG HCCCCHHHHHHHCCC	8.83	23312004
371	Methylation	DNSEEYIRRDLEGSD CCCHHHHHHHCCCCC	25.76	-
377	Phosphorylation	IRRDLEGSDIDTRRR HHHHCCCCCHHHHHH	23.24	20873877
381	Phosphorylation	LEGSDIDTRRRAACD CCCCCHHHHHHHHHH	26.81	21712546
387	S-nitrosocysteine	DTRRRAACDLVRGLC HHHHHHHHHHHHHHH	3.97	-
387	S-nitrosylation	DTRRRAACDLVRGLC HHHHHHHHHHHHHHH	3.97	19483679
408	Phosphorylation	VTGIFSGYVNSMLQE CHHHHHHHHHHHHHH	8.68	-
421	Phosphorylation	QEYAKNPSVNWKHKD HHHHHCCCCCCCHHH	37.16	20873877
425	Ubiquitination	KNPSVNWKHKDAAIY HCCCCCCCHHHHHHH	35.26	-
425	2-Hydroxyisobutyrylation	KNPSVNWKHKDAAIY HCCCCCCCHHHHHHH	35.26	-
425	Acetylation	KNPSVNWKHKDAAIY HCCCCCCCHHHHHHH	35.26	26210075
432	Phosphorylation	KHKDAAIYLVTSLAS CHHHHHHHHHHHHHH	7.15	28152594
435	Phosphorylation	DAAIYLVTSLASKAQ HHHHHHHHHHHHHHH	18.54	23286773
440	Ubiquitination	LVTSLASKAQTQKHG HHHHHHHHHHHHHCC	38.62	21890473
440	Ubiquitination	LVTSLASKAQTQKHG HHHHHHHHHHHHHCC	38.62	21890473
440	Acetylation	LVTSLASKAQTQKHG HHHHHHHHHHHHHCC	38.62	25953088
440 (in isoform 1)	Ubiquitination	-	38.62	21890473
440 (in isoform 3)	Ubiquitination	-	38.62	21890473
445	Ubiquitination	ASKAQTQKHGITQAN HHHHHHHHCCCCHHH	47.38	-
471	Phosphorylation	HILPDLKSANVNEFP HHHHCHHCCCCCCCC	32.16	21712546
481	Ubiquitination	VNEFPVLKADGIKYI CCCCCEEECCCCEEE	44.67	21906983
481	2-Hydroxyisobutyrylation	VNEFPVLKADGIKYI CCCCCEEECCCCEEE	44.67	-
481 (in isoform 1)	Ubiquitination	-	44.67	21890473
481 (in isoform 3)	Ubiquitination	-	44.67	21890473
487	Phosphorylation	LKADGIKYIMIFRNQ EECCCCEEEEEECCC	8.19	23882029
518	Acetylation	LQAESIVVHTYAAHA HCHHHHHHHHHHHHH	2.38	19608861
562	Phosphorylation	TNLFKALTLPGSSEN HHHHHHHCCCCCCHH	35.45	27251275
566	Phosphorylation	KALTLPGSSENEYIM HHHCCCCCCHHHHHH	32.32	27251275
567	Phosphorylation	ALTLPGSSENEYIMK HHCCCCCCHHHHHHH	50.81	27251275
571	Phosphorylation	PGSSENEYIMKAIMR CCCCHHHHHHHHHHH	20.21	27251275
574	Acetylation	SENEYIMKAIMRSFS CHHHHHHHHHHHHHH	25.79	19608861
698	Phosphorylation	QPVLWERTGNIPALV HHHHHHHHCCHHHHH	24.06	23312004
721	Phosphorylation	RGSNTIASAAADKIP CCCCHHHHHHHHHCC	18.00	20068231
726	Ubiquitination	IASAAADKIPGLLGV HHHHHHHHCCHHHHH	46.18	21890473
726	Ubiquitination	IASAAADKIPGLLGV HHHHHHHHCCHHHHH	46.18	21890473
726	Acetylation	IASAAADKIPGLLGV HHHHHHHHCCHHHHH	46.18	26051181
726 (in isoform 1)	Ubiquitination	-	46.18	21890473
726 (in isoform 3)	Ubiquitination	-	46.18	21890473
768	Acetylation	ESVDQYRKQIFILLF HHHHHHHHHHHHHHH	42.69	19608861
768	Ubiquitination	ESVDQYRKQIFILLF HHHHHHHHHHHHHHH	42.69	19608861
781	Phosphorylation	LFQRLQNSKTTKFIK HHHHHCCCCCHHHHH	20.58	26074081
783	Phosphorylation	QRLQNSKTTKFIKSF HHHCCCCCHHHHHHH	34.73	26074081
784	Phosphorylation	RLQNSKTTKFIKSFL HHCCCCCHHHHHHHH	27.91	26074081
789	Phosphorylation	KTTKFIKSFLVFINL CCHHHHHHHHHHHHH	20.99	24667141
797	Phosphorylation	FLVFINLYCIKYGAL HHHHHHHHHHHHHHH	6.40	24667141
824	Acetylation	MFGMVLEKIIIPEIQ HHHHHHHHHHHHHHH	34.74	19608861
824	Ubiquitination	MFGMVLEKIIIPEIQ HHHHHHHHHHHHHHH	34.74	21890473
824	Ubiquitination	MFGMVLEKIIIPEIQ HHHHHHHHHHHHHHH	34.74	21890473
824 (in isoform 1)	Ubiquitination	-	34.74	21890473
824 (in isoform 3)	Ubiquitination	-	34.74	21890473
832	Ubiquitination	IIIPEIQKVSGNVEK HHHHHHHHCCCCCCH	43.99	-
832	Acetylation	IIIPEIQKVSGNVEK HHHHHHHHCCCCCCH	43.99	23236377
834	Phosphorylation	IPEIQKVSGNVEKKI HHHHHHCCCCCCHHH	31.52	21601212
839	2-Hydroxyisobutyrylation	KVSGNVEKKICAVGI HCCCCCCHHHHHHHH	43.06	-
840	Ubiquitination	VSGNVEKKICAVGIT CCCCCCHHHHHHHHH	29.52	-
842	Glutathionylation	GNVEKKICAVGITKL CCCCHHHHHHHHHHH	3.26	22555962
848	Ubiquitination	ICAVGITKLLTECPP HHHHHHHHHHHHCCC	39.31	-
848	Acetylation	ICAVGITKLLTECPP HHHHHHHHHHHHCCC	39.31	26051181
853	Glutathionylation	ITKLLTECPPMMDTE HHHHHHHCCCCCCCH	3.74	22555962
853	S-palmitoylation	ITKLLTECPPMMDTE HHHHHHHCCCCCCCH	3.74	26865113
856	Sulfoxidation	LLTECPPMMDTEYTK HHHHCCCCCCCHHHH	1.99	30846556
857	Sulfoxidation	LTECPPMMDTEYTKL HHHCCCCCCCHHHHH	7.71	30846556
862	Phosphorylation	PMMDTEYTKLWTPLL CCCCCHHHHHHHHHH	17.27	20860994
904	Phosphorylation	PGYQTAFSQLAFAGK CCHHHHHHHHHHCCC	23.09	-
912	Ubiquitination	QLAFAGKKEHDPVGQ HHHHCCCCCCCCHHH	60.40	-
920	Sulfoxidation	EHDPVGQMVNNPKIH CCCCHHHHCCCCHHH	2.61	21406390
925	Ubiquitination	GQMVNNPKIHLAQSL HHHCCCCHHHHHHHH	44.90	21890473
925	Ubiquitination	GQMVNNPKIHLAQSL HHHCCCCHHHHHHHH	44.90	21890473
925 (in isoform 1)	Ubiquitination	-	44.90	21890473
925 (in isoform 3)	Ubiquitination	-	44.90	21890473
931	Phosphorylation	PKIHLAQSLHKLSTA CHHHHHHHHHHHHCC	27.17	23401153
934	Ubiquitination	HLAQSLHKLSTACPG HHHHHHHHHHCCCCC	49.80	21890473
934	Ubiquitination	HLAQSLHKLSTACPG HHHHHHHHHHCCCCC	49.80	21890473
934	Acetylation	HLAQSLHKLSTACPG HHHHHHHHHHCCCCC	49.80	25953088
934 (in isoform 1)	Ubiquitination	-	49.80	21890473
934 (in isoform 3)	Ubiquitination	-	49.80	21890473
936	Phosphorylation	AQSLHKLSTACPGRV HHHHHHHHCCCCCCC	20.82	20873877
937	Phosphorylation	QSLHKLSTACPGRVP HHHHHHHCCCCCCCC	42.59	20873877
939	S-nitrosocysteine	LHKLSTACPGRVPSM HHHHHCCCCCCCCHH	3.58	-
939	S-nitrosylation	LHKLSTACPGRVPSM HHHHHCCCCCCCCHH	3.58	19483679
945	Phosphorylation	ACPGRVPSMVSTSLN CCCCCCCHHHCCCCC	29.03	-
946	Sulfoxidation	CPGRVPSMVSTSLNA CCCCCCHHHCCCCCH	1.95	30846556

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
-	K	Ubiquitination	E3 ubiquitin ligase	BIRC2	Q13490	PMID:26668314

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of XPO2_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 XPO2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TMM62_HUMAN	TMEM62	physical	16169070
HNRPL_HUMAN	HNRNPL	physical	16169070
IMA5_HUMAN	KPNA1	physical	10523667
IMA1_HUMAN	KPNA2	physical	10523667
IMA3_HUMAN	KPNA4	physical	10523667
BCCIP_HUMAN	BCCIP	physical	22863883
KCRB_HUMAN	CKB	physical	22863883
CNDP2_HUMAN	CNDP2	physical	22863883
GUAD_HUMAN	GDA	physical	22863883
PSF3_HUMAN	GINS3	physical	22863883
KYNU_HUMAN	KYNU	physical	22863883
LDHA_HUMAN	LDHA	physical	22863883
MVD1_HUMAN	MVD	physical	22863883
PSA_HUMAN	NPEPPS	physical	22863883
KS6A3_HUMAN	RPS6KA3	physical	22863883
SCLY_HUMAN	SCLY	physical	22863883
NHRF1_HUMAN	SLC9A3R1	physical	22863883
SPSY_HUMAN	SMS	physical	22863883
TBCB_HUMAN	TBCB	physical	22863883
TGM2_HUMAN	TGM2	physical	22863883
UBFD1_HUMAN	UBFD1	physical	22863883
CADH1_HUMAN	CDH1	physical	20734115
CYB5B_HUMAN	CYB5B	physical	26344197
EF2_HUMAN	EEF2	physical	26344197
HNRPF_HUMAN	HNRNPF	physical	26344197
RAN_HUMAN	RAN	physical	26344197
ST1C3_HUMAN	SULT1C3	physical	26344197
ST1C4_HUMAN	SULT1C4	physical	26344197
TIPRL_HUMAN	TIPRL	physical	26344197
TPP2_HUMAN	TPP2	physical	26344197
UN45A_HUMAN	UNC45A	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 XPO2_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 MET-1, 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-158; LYS-574 AND LYS-824,AND MASS SPECTROMETRY.	19608861 [Abstract]