IPO5_MOUSE - dbPTM
IPO5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IPO5_MOUSE
UniProt AC Q8BKC5
Protein Name Importin-5
Gene Name Ipo5
Organism Mus musculus (Mouse).
Sequence Length 1097
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the 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 the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Binds to CPEB3 and mediates its nuclear import following neuronal stimulation. [PubMed: 22730302]
Protein Sequence MAAAAAEQQQFYLLLGNLLSPDNVVRKQAEETYENIPGRSKITFLLQAIRNTTAAEEARQMAAVLLRRLLSSAFDEVYPALPSDVQTAIKSELLMIIQMETQSSMRKKICDIAAELARNLIDEDGNNQWPEGLKFLFDSVSSQNMGLREAALHIFWNFPGIFGNQQQHYLDVIKRMLVQCMQDQEHPSIRTLSARATAAFILANEHNVALFKHFADLLPGFLQAVNDSCYQNDDSVLKSLVEIADTVPKYLRPHLEATLQLSLKLCGDTNLNNMQRQLALEVIVTLSETAAAMLRKHTSLIAQTIPQMLAMMVDLEEDEDWANADELEDDDFDSNAVAGESALDRMACGLGGKLVLPMIKEHIMQMLQNPDWKYRHAGLMALSAIGEGCHQQMEGILNEIVNFVLLFLQDPHPRVRYAACNAVGQMATDFAPGFQKKFHEKVIAALLQTMEDQGNQRVQAHAAAALINFTEDCPKSLLIPYLDNLVKHLHSIMVLKLQELIQKGTKLVLEQVVTSIASVADTAEEKFVPYYDLFMPSLKHIVENAVQKELRLLRGKTIECISLIGLAVGKEKFMQDASDVMQLLLKTQTDFNDMEDDDPQISYMISAWARMCKILGKEFQQYLPVVMGPLMKTASIKPEVALLDTQDMENMSDDDGWEFVNLGDQQSFGIKTAGLEEKSTACQMLVCYAKELKEGFVEYTEQVVKLMVPLLKFYFHDGVRVAAAESMPLLLECARVRGPEYLTQMWHFMCDALIKAIGTEPDSDVLSEIMHSFAKCIEVMGDGCLNNEHFEELGGILKAKLEEHFKNQELRQVKRQDEDYDEQVEESLQDEDDNDVYILTKVSDILHSIFSSYKEKVLPWFEQLLPLIVNLICPQRPWPDRQWGLCIFDDIVEHCSPASFKYAEYFISPMLQYVCDNSPEVRQAAAYGLGVMAQFGGDNYRPFCTDALPLLVRVIQAPEAKTKENVNATENCISAVGKIMKFKPDCVNVEEVLPHWLSWLPLHEDKEEAVQTFSYLCDLIESNHPIVLGPNNTNLPKIFSIIAEGEMHEAIKHEDPCAKRLANVVRQVQTSGGLWTECIAQLSPEQQAAIQELLNSA
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
2Acetylation------MAAAAAEQQ
------CCHHHHHHH
19.67-
12PhosphorylationAAEQQQFYLLLGNLL
HHHHHHHHHHHHHCC
7.6629233185
27UbiquitinationSPDNVVRKQAEETYE
CCCHHHHHHHHHHHH
42.1022790023
40PhosphorylationYENIPGRSKITFLLQ
HHCCCCHHHHHHHHH
34.0330635358
41AcetylationENIPGRSKITFLLQA
HCCCCHHHHHHHHHH
44.3922826441
108UbiquitinationTQSSMRKKICDIAAE
CCHHHHHHHHHHHHH
37.9022790023
266S-nitrosocysteineLQLSLKLCGDTNLNN
HHHHHHHHCCCCCHH
4.42-
266S-palmitoylationLQLSLKLCGDTNLNN
HHHHHHHHCCCCCHH
4.4228526873
266S-nitrosylationLQLSLKLCGDTNLNN
HHHHHHHHCCCCCHH
4.4221278135
441AcetylationFQKKFHEKVIAALLQ
HHHHHHHHHHHHHHH
30.3022826441
449PhosphorylationVIAALLQTMEDQGNQ
HHHHHHHHHHHHCCH
23.6125159016
476PhosphorylationFTEDCPKSLLIPYLD
CCCCCCHHHHHHHHH
17.3526643407
488UbiquitinationYLDNLVKHLHSIMVL
HHHHHHHHHHHHHHH
22.6927667366
518PhosphorylationQVVTSIASVADTAEE
HHHHHHHHHHHHHHH
19.0326824392
548UbiquitinationIVENAVQKELRLLRG
HHHHHHHHHHHHHCC
52.7122790023
548AcetylationIVENAVQKELRLLRG
HHHHHHHHHHHHHCC
52.7122826441
556UbiquitinationELRLLRGKTIECISL
HHHHHCCCCHHHHHH
39.64-
578PhosphorylationEKFMQDASDVMQLLL
HHHCCCHHHHHHHHH
38.7420139300
613UbiquitinationSAWARMCKILGKEFQ
HHHHHHHHHHCHHHH
31.46-
633PhosphorylationVMGPLMKTASIKPEV
HHCCHHCCCCCCCCE
16.2123984901
635PhosphorylationGPLMKTASIKPEVAL
CCHHCCCCCCCCEEE
36.0523984901
645PhosphorylationPEVALLDTQDMENMS
CCEEEECCCCCCCCC
26.8326239621
652PhosphorylationTQDMENMSDDDGWEF
CCCCCCCCCCCCCEE
49.8529514104
667PhosphorylationVNLGDQQSFGIKTAG
EECCCHHCCCCCCCC
21.58-
690AcetylationQMLVCYAKELKEGFV
HHHHHHHHHHHCCHH
36.7822826441
693AcetylationVCYAKELKEGFVEYT
HHHHHHHHCCHHHHH
57.8122826441
733S-palmitoylationSMPLLLECARVRGPE
HHHHHHHHHHHHCHH
2.7128526873
733S-nitrosocysteineSMPLLLECARVRGPE
HHHHHHHHHHHHCHH
2.71-
733S-nitrosylationSMPLLLECARVRGPE
HHHHHHHHHHHHCHH
2.7121278135
740UbiquitinationCARVRGPEYLTQMWH
HHHHHCHHHHHHHHH
56.8727667366
743PhosphorylationVRGPEYLTQMWHFMC
HHCHHHHHHHHHHHH
18.5729514104
766UbiquitinationTEPDSDVLSEIMHSF
CCCCHHHHHHHHHHH
4.5727667366
767PhosphorylationEPDSDVLSEIMHSFA
CCCHHHHHHHHHHHH
25.5622807455
800UbiquitinationLGGILKAKLEEHFKN
HHHHHHHHHHHHHCC
55.6427667366
820PhosphorylationVKRQDEDYDEQVEES
HHHCCCCHHHHHHHH
21.2324224561
826UbiquitinationDYDEQVEESLQDEDD
CHHHHHHHHHCCCCC
58.8727667366
827PhosphorylationYDEQVEESLQDEDDN
HHHHHHHHHCCCCCC
20.1621082442
972S-nitrosylationNVNATENCISAVGKI
CCCCCHHHHHHHHHH
1.8021278135
972GlutathionylationNVNATENCISAVGKI
CCCCCHHHHHHHHHH
1.8024333276
972S-nitrosocysteineNVNATENCISAVGKI
CCCCCHHHHHHHHHH
1.80-

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 IPO5_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IPO5_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 IPO5_MOUSE !!

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

Oops, there are no PPI records of IPO5_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IPO5_MOUSE

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Related Literatures of Post-Translational Modification

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