IPO7_HUMAN - dbPTM
IPO7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IPO7_HUMAN
UniProt AC O95373
Protein Name Importin-7
Gene Name IPO7
Organism Homo sapiens (Human).
Sequence Length 1038
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Functions in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with KPNB1 mediates the nuclear import of H1 histone and the Ran-binding site of IPO7 is not required but synergizes with that of KPNB1 in importin/substrate complex dissociation. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones.; (Microbial infection) Mediates the nuclear import of HIV-1 reverse transcription complex (RTC) integrase. Binds and mediates the nuclear import of HIV-1 Rev..
Protein Sequence MDPNTIIEALRGTMDPALREAAERQLNEAHKSLNFVSTLLQITMSEQLDLPVRQAGVIYLKNMITQYWPDRETAPGDISPYTIPEEDRHCIRENIVEAIIHSPELIRVQLTTCIHHIIKHDYPSRWTAIVDKIGFYLQSDNSACWLGILLCLYQLVKNYEYKKPEERSPLVAAMQHFLPVLKDRFIQLLSDQSDQSVLIQKQIFKIFYALVQYTLPLELINQQNLTEWIEILKTVVNRDVPNETLQVEEDDRPELPWWKCKKWALHILARLFERYGSPGNVSKEYNEFAEVFLKAFAVGVQQVLLKVLYQYKEKQYMAPRVLQQTLNYINQGVSHALTWKNLKPHIQGIIQDVIFPLMCYTDADEELWQEDPYEYIRMKFDVFEDFISPTTAAQTLLFTACSKRKEVLQKTMGFCYQILTEPNADPRKKDGALHMIGSLAEILLKKKIYKDQMEYMLQNHVFPLFSSELGYMRARACWVLHYFCEVKFKSDQNLQTALELTRRCLIDDREMPVKVEAAIALQVLISNQEKAKEYITPFIRPVMQALLHIIRETENDDLTNVIQKMICEYSEEVTPIAVEMTQHLAMTFNQVIQTGPDEEGSDDKAVTAMGILNTIDTLLSVVEDHKEITQQLEGICLQVIGTVLQQHVLEFYEEIFSLAHSLTCQQVSPQMWQLLPLVFEVFQQDGFDYFTDMMPLLHNYVTVDTDTLLSDTKYLEMIYSMCKKVLTGVAGEDAECHAAKLLEVIILQCKGRGIDQCIPLFVEAALERLTREVKTSELRTMCLQVAIAALYYNPHLLLNTLENLRFPNNVEPVTNHFITQWLNDVDCFLGLHDRKMCVLGLCALIDMEQIPQVLNQVSGQILPAFILLFNGLKRAYACHAEHENDSDDDDEAEDDDETEELGSDEDDIDEDGQEYLEILAKQAGEDGDDEDWEEDDAEETALEGYSTIIDDEDNPVDEYQIFKAIFQTIQNRNPVWYQALTHGLNEEQRKQLQDIATLADQRRAAHESKMIEKHGGYKFSAPVVPSSFNFGGPAPGMN
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 Orthologous
Protein Cluster
1Acetylation-------MDPNTIIE
-------CCHHHHHH		63.5619413330
1Sulfoxidation-------MDPNTIIE
-------CCHHHHHH		63.5628465586
5Phosphorylation---MDPNTIIEALRG
---CCHHHHHHHHHC		28.8122210691
5O-linked_Glycosylation---MDPNTIIEALRG
---CCHHHHHHHHHC		28.8123301498
11MethylationNTIIEALRGTMDPAL
HHHHHHHHCCCCHHH		45.65115480385
14SulfoxidationIEALRGTMDPALREA
HHHHHCCCCHHHHHH		6.9130846556
32PhosphorylationQLNEAHKSLNFVSTL
HHHHHHHHHCHHHHH		20.7620068231
37PhosphorylationHKSLNFVSTLLQITM
HHHHCHHHHHHHHHH		14.8120068231
38PhosphorylationKSLNFVSTLLQITMS
HHHCHHHHHHHHHHH		26.6220068231
43PhosphorylationVSTLLQITMSEQLDL
HHHHHHHHHHHCCCC		11.1520068231
44SulfoxidationSTLLQITMSEQLDLP
HHHHHHHHHHCCCCC		4.4228183972
45PhosphorylationTLLQITMSEQLDLPV
HHHHHHHHHCCCCCH		17.3420068231
59PhosphorylationVRQAGVIYLKNMITQ
HHHCCEEEEHHCHHH		14.82-
61UbiquitinationQAGVIYLKNMITQYW
HCCEEEEHHCHHHHC		27.74-
79PhosphorylationETAPGDISPYTIPEE
CCCCCCCCCCCCCHH		19.3227732954
81PhosphorylationAPGDISPYTIPEEDR
CCCCCCCCCCCHHHH		15.5427732954
82PhosphorylationPGDISPYTIPEEDRH
CCCCCCCCCCHHHHH		33.1827732954
102O-linked_GlycosylationIVEAIIHSPELIRVQ
HHHHHHCCHHHHHHH		15.0623301498
102PhosphorylationIVEAIIHSPELIRVQ
HHHHHHCCHHHHHHH		15.0627251275
142PhosphorylationFYLQSDNSACWLGIL
HHHCCCCCHHHHHHH		29.78-
1822-HydroxyisobutyrylationQHFLPVLKDRFIQLL
HHHHHHHHHHHHHHH		47.28-
182UbiquitinationQHFLPVLKDRFIQLL
HHHHHHHHHHHHHHH		47.28-
201UbiquitinationDQSVLIQKQIFKIFY
CCHHHHHHHHHHHHH		38.07-
259UbiquitinationRPELPWWKCKKWALH
CCCCCHHHHHHHHHH		32.10-
275PhosphorylationLARLFERYGSPGNVS
HHHHHHHHCCCCCCC		18.1126552605
277PhosphorylationRLFERYGSPGNVSKE
HHHHHHCCCCCCCHH		22.2426552605
282PhosphorylationYGSPGNVSKEYNEFA
HCCCCCCCHHHHHHH		24.6226552605
283UbiquitinationGSPGNVSKEYNEFAE
CCCCCCCHHHHHHHH		60.9921906983
285PhosphorylationPGNVSKEYNEFAEVF
CCCCCHHHHHHHHHH		24.5926552605
309PhosphorylationQVLLKVLYQYKEKQY
HHHHHHHHHHHHHHC		16.8828152594
311PhosphorylationLLKVLYQYKEKQYMA
HHHHHHHHHHHHCCC		13.9320860994
312SuccinylationLKVLYQYKEKQYMAP
HHHHHHHHHHHCCCH		42.8023954790
312UbiquitinationLKVLYQYKEKQYMAP
HHHHHHHHHHHCCCH		42.80-
312AcetylationLKVLYQYKEKQYMAP
HHHHHHHHHHHCCCH		42.8026051181
3142-HydroxyisobutyrylationVLYQYKEKQYMAPRV
HHHHHHHHHCCCHHH		42.45-
316PhosphorylationYQYKEKQYMAPRVLQ
HHHHHHHCCCHHHHH		13.3024043423
325PhosphorylationAPRVLQQTLNYINQG
CHHHHHHHHHHHHHH		12.1924043423
328PhosphorylationVLQQTLNYINQGVSH
HHHHHHHHHHHHHHH		12.3624043423
334PhosphorylationNYINQGVSHALTWKN
HHHHHHHHHHHCCCC		15.1824043423
338PhosphorylationQGVSHALTWKNLKPH
HHHHHHHCCCCCHHH		34.8724043423
373PhosphorylationELWQEDPYEYIRMKF
HHHCCCCHHHHHHHH		33.42-
379"N6,N6-dimethyllysine"PYEYIRMKFDVFEDF
CHHHHHHHHHHCCCC		28.67-
379MethylationPYEYIRMKFDVFEDF
CHHHHHHHHHHCCCC		28.67-
403"N6,N6-dimethyllysine"LLFTACSKRKEVLQK
HHHHHHHHHHHHHHH		68.33-
403MethylationLLFTACSKRKEVLQK
HHHHHHHHHHHHHHH		68.33-
428UbiquitinationEPNADPRKKDGALHM
CCCCCCCCCCCHHHH		61.68-
429UbiquitinationPNADPRKKDGALHMI
CCCCCCCCCCHHHHH		63.77-
438PhosphorylationGALHMIGSLAEILLK
CHHHHHHHHHHHHHH		17.3020068231
445MethylationSLAEILLKKKIYKDQ
HHHHHHHHCCCCHHH		48.88-
446MethylationLAEILLKKKIYKDQM
HHHHHHHCCCCHHHH		44.35-
489UbiquitinationYFCEVKFKSDQNLQT
HHHEEECCCCCCHHH		47.61-
489AcetylationYFCEVKFKSDQNLQT
HHHEEECCCCCCHHH		47.6126051181
490PhosphorylationFCEVKFKSDQNLQTA
HHEEECCCCCCHHHH		47.7821712546
609SulfoxidationDDKAVTAMGILNTID
CCHHHHHHHHHHHHH		2.2130846556
700PhosphorylationMMPLLHNYVTVDTDT
HHHHHCCCEEECCCH		6.1726074081
702PhosphorylationPLLHNYVTVDTDTLL
HHHCCCEEECCCHHC		11.4226074081
705PhosphorylationHNYVTVDTDTLLSDT
CCCEEECCCHHCCCC		26.9226074081
714PhosphorylationTLLSDTKYLEMIYSM
HHCCCCHHHHHHHHH		15.2423663014
719PhosphorylationTKYLEMIYSMCKKVL
CHHHHHHHHHHHHHH		6.7723663014
720PhosphorylationKYLEMIYSMCKKVLT
HHHHHHHHHHHHHHH		13.5423663014
724UbiquitinationMIYSMCKKVLTGVAG
HHHHHHHHHHHCCCC		37.23-
7242-HydroxyisobutyrylationMIYSMCKKVLTGVAG
HHHHHHHHHHHCCCC		37.23-
757GlutathionylationKGRGIDQCIPLFVEA
CCCCHHHHHHHHHHH		2.8422555962
774UbiquitinationERLTREVKTSELRTM
HHHHHHCCHHHHHHH		41.39-
775PhosphorylationRLTREVKTSELRTMC
HHHHHCCHHHHHHHH		32.39-
876PhosphorylationFNGLKRAYACHAEHE
HHHHHHHHHHHCCCC		17.5017081983
886PhosphorylationHAEHENDSDDDDEAE
HCCCCCCCCCCCCCC		55.3017081983
898PhosphorylationEAEDDDETEELGSDE
CCCCCHHHHHHCCCC		41.5817081983
903PhosphorylationDETEELGSDEDDIDE
HHHHHHCCCCHHCCC		50.9117081983
915PhosphorylationIDEDGQEYLEILAKQ
CCCCHHHHHHHHHHH		11.1817192257
959PhosphorylationEDNPVDEYQIFKAIF
CCCCCCHHHHHHHHH		11.49-
977PhosphorylationQNRNPVWYQALTHGL
HHCCHHHHHHHHCCC		5.5527642862
990UbiquitinationGLNEEQRKQLQDIAT
CCCHHHHHHHHHHHH		55.8721906983
1009UbiquitinationRRAAHESKMIEKHGG
HHHHHHHHHHHHHCC		40.69-
10092-HydroxyisobutyrylationRRAAHESKMIEKHGG
HHHHHHHHHHHHHCC		40.69-
1013AcetylationHESKMIEKHGGYKFS
HHHHHHHHHCCCCCC		36.3026210075
1013UbiquitinationHESKMIEKHGGYKFS
HHHHHHHHHCCCCCC		36.30-
10132-HydroxyisobutyrylationHESKMIEKHGGYKFS
HHHHHHHHHCCCCCC		36.30-
1017PhosphorylationMIEKHGGYKFSAPVV
HHHHHCCCCCCCCCC		17.2923090842
1018AcetylationIEKHGGYKFSAPVVP
HHHHCCCCCCCCCCC		35.8026051181
1018UbiquitinationIEKHGGYKFSAPVVP
HHHHCCCCCCCCCCC		35.80-
1020PhosphorylationKHGGYKFSAPVVPSS
HHCCCCCCCCCCCCC		27.7522777824
1026PhosphorylationFSAPVVPSSFNFGGP
CCCCCCCCCCCCCCC		35.6323090842
1027PhosphorylationSAPVVPSSFNFGGPA
CCCCCCCCCCCCCCC		20.3824719451
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 IPO7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IPO7_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 IPO7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAN_HUMANRANphysical
9214382
MPP10_HUMANMPHOSPH10physical
26344197
PPM1G_HUMANPPM1Gphysical
26344197
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 IPO7_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 1-11, AND ACETYLATION AT MET-1.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-876; SER-886; THR-898AND SER-903, AND MASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311, AND MASSSPECTROMETRY.

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