IPO7_MOUSE - dbPTM
IPO7_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IPO7_MOUSE
UniProt AC Q9EPL8
Protein Name Importin-7
Gene Name Ipo7
Organism Mus musculus (Mouse).
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. 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 (By similarity). In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones..
Protein Sequence MDPNTIIEALRGTMDPALREAAERQLNEAHKSLNFVSTLLQITMSEQLDLPVRQAGVIYLKNMITQYWPDREATPGDIAPYTIPEEDRHCIRENIVEAIIHSPELIRVQLTTCIHHIIKHDYPSRWTAIVDKIGFYLQSDNSACWLGILLCLYQLVKNYEYKKPEERSPLVAAMQHFLPVLKDRFIQLLSDQSDQSVLIQKQIFKIFYALVQYTLPLELINQQNLTEWVEILKTVVNRDVPNETLQVEEDDRPELPWWKCKKWALHILARLFERYGSPGNVSKEYNEFAEVFLKAFAVGVQQVLLKVLYQYKEKQYMAPRVLQQTLNYINQGVSHALTWKNLKPHIQGIIQDVIFPLMCYTDADEELWQEDPYEYIRMKFDVFEDFISPTTAAQTLLFTACSKRKEVLQKTMGFCYQILTEPNADPRKKDGALHMIGSLAEILLKKKIYKDQMEYMLQNHVFPLFSSELGYMRARACWVLHYFCEVKFKSDQNLQTALELTRRCLIDDREMPVKVEAAIALQVLISNQEKAKEYITPFIRPVMQALLHIIRETENDDLTNVIQKMICEYSEEVTPIAVEMTQHLAMTFNQVIQTGPDEEGSDDKAVTAMGILNTIDTLLSVVEDHKEITQQLEGICLQVIGTVLQQHVLEFYEEIFSLAHSLTCQQVSPQMWQLLPLVFEVFQQDGFDYFTDMMPLLHNYVTVDTDTLLSDTKYLEMIYSMCKKVLTGVAGEDAECHAAKLLEVIILQCKGRGIDQCIPLFVEAALERLTREVKTSELRTMCLQVAIAALYYNPHLLLNTLENLRFPNNVEPVTNHFITQWLNDVDCFLGLHDRKMCVLGLCALIDMEQIPQVLNQVSGQILPAFILLFNGLKRAYACHAEHENDSDDDEDAEDDDETEELGSDEDDIDEDGQEYLEILAKQAGEDGDDEDWEEDDAEETALEGYSTIIDDEDNPVDEYQIFKAIFQTIQNRNPVWYQALTHGLNEEQRKQLQDIATLADQRRAAHESKMIEKHGGYKFSAPVVPSSFNFGGPAPGMN
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
63.56-
5Phosphorylation---MDPNTIIEALRG
---CCHHHHHHHHHC
28.8127180971
37PhosphorylationHKSLNFVSTLLQITM
HHHHCHHHHHHHHHH
14.8128059163
45PhosphorylationTLLQITMSEQLDLPV
HHHHHHHHHCCCCCH
17.3428059163
283UbiquitinationGSPGNVSKEYNEFAE
CCCCCCCHHHHHHHH
60.99-
410AcetylationKRKEVLQKTMGFCYQ
HHHHHHHHHHCHHHH
36.0023201123
477S-nitrosocysteineGYMRARACWVLHYFC
HHHHHHHHHHHHHHH
1.84-
477S-nitrosylationGYMRARACWVLHYFC
HHHHHHHHHHHHHHH
1.8420925432
668PhosphorylationSLTCQQVSPQMWQLL
HCHHCCCCHHHHHHH
12.70-
757S-nitrosocysteineKGRGIDQCIPLFVEA
CCCCHHHHHHHHHHH
2.84-
757S-nitrosylationKGRGIDQCIPLFVEA
CCCCHHHHHHHHHHH
2.8421278135
757GlutathionylationKGRGIDQCIPLFVEA
CCCCHHHHHHHHHHH
2.8424333276
876PhosphorylationFNGLKRAYACHAEHE
HHHHHHHHHHHCCCC
17.5025159016
886PhosphorylationHAEHENDSDDDEDAE
HCCCCCCCCCCCCCC
55.3025159016
898PhosphorylationDAEDDDETEELGSDE
CCCCCHHHHHHCCCC
41.5823737553
903PhosphorylationDETEELGSDEDDIDE
HHHHHHCCCCHHCCC
50.9125159016
915PhosphorylationIDEDGQEYLEILAKQ
CCCCHHHHHHHHHHH
11.1823737553
990UbiquitinationGLNEEQRKQLQDIAT
CCCHHHHHHHHHHHH
55.8722790023
1017PhosphorylationMIEKHGGYKFSAPVV
HHHHHCCCCCCCCCC
17.2925266776
1018UbiquitinationIEKHGGYKFSAPVVP
HHHHCCCCCCCCCCC
35.80-
1020PhosphorylationKHGGYKFSAPVVPSS
HHCCCCCCCCCCCCC
27.7525266776

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IPO7_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of IPO7_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IPO7_MOUSE

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Related Literatures of Post-Translational Modification

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