IPO8_HUMAN - dbPTM
IPO8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IPO8_HUMAN
UniProt AC O15397
Protein Name Importin-8
Gene Name IPO8
Organism Homo sapiens (Human).
Sequence Length 1037
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Seems to function 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. In vitro mediates the nuclear import of SRP19..
Protein Sequence MDLNRIIQALKGTIDPKLRIAAENELNQSYKIINFAPSLLRIIVSDHVEFPVRQAAAIYLKNMVTQYWPDREPPPGEAIFPFNIHENDRQQIRDNIVEGIIRSPDLVRVQLTMCLRAIIKHDFPGHWPGVVDKIDYYLQSQSSASWLGSLLCLYQLVKTYEYKKAEEREPLIIAMQIFLPRIQQQIVQLLPDSSYYSVLLQKQILKIFYALVQYALPLQLVNNQTMTTWMEIFRTIIDRTVPPETLHIDEDDRPELVWWKCKKWALHIVARLFERYGSPGNVTKEYFEFSEFFLKTYAVGIQQVLLKILDQYRQKEYVAPRVLQQAFNYLNQGVVHSITWKQMKPHIQNISEDVIFSVMCYKDEDEELWQEDPYEYIRMKFDIFEDYASPTTAAQTLLYTAAKKRKEVLPKMMAFCYQILTDPNFDPRKKDGALHVIGSLAEILLKKSLFKDQMELFLQNHVFPLLLSNLGYLRARSCWVLHAFSSLKFHNELNLRNAVELAKKSLIEDKEMPVKVEAALALQSLISNQIQAKEYMKPHVRPIMQELLHIVRETENDDVTNVIQKMICEYSQEVASIAVDMTQHLAEIFGKVLQSDEYEEVEDKTVMAMGILHTIDTILTVVEDHKEITQQLENICLRIIDLVLQKHVIEFYEEILSLAYSLTCHSISPQMWQLLGILYEVFQQDCFEYFTDMMPLLHNYVTIDTDTLLSNAKHLEILFTMCRKVLCGDAGEDAECHAAKLLEVIILQCKGRGIDQCIPLFVQLVLERLTRGVKTSELRTMCLQVAIAALYYNPDLLLHTLERIQLPHNPGPITVQFINQWMNDTDCFLGHHDRKMCIIGLSILLELQNRPPAVDAVVGQIVPSILFLFLGLKQVCATRQLVNREDRSKAEKADMEENEEISSDEEETNVTAQAMQSNNGRGEDEEEEDDDWDEEVLEETALEGFSTPLDLDNSVDEYQFFTQALITVQSRDAAWYQLLMAPLSEDQRTALQEVYTLAEHRRTVAEAKKKIEQQGGFTFENKGVLSAFNFGTVPSNN
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
11UbiquitinationNRIIQALKGTIDPKL
HHHHHHHCCCCCHHH		57.9629967540
13PhosphorylationIIQALKGTIDPKLRI
HHHHHCCCCCHHHHH		22.18-
17UbiquitinationLKGTIDPKLRIAAEN
HCCCCCHHHHHHHHC		46.8029967540
30PhosphorylationENELNQSYKIINFAP
HCHHCHHHHHHHCCH		9.1025159151
31UbiquitinationNELNQSYKIINFAPS
CHHCHHHHHHHCCHH		42.2122817900
103PhosphorylationIVEGIIRSPDLVRVQ
HHHHHHHCCCHHHHH		16.6221406692
110UbiquitinationSPDLVRVQLTMCLRA
CCCHHHHHHHHHHHH		22.2024816145
112PhosphorylationDLVRVQLTMCLRAII
CHHHHHHHHHHHHHH		6.6921406692
160PhosphorylationLYQLVKTYEYKKAEE
HHHHHHHCCHHCHHH		16.1429759185
162PhosphorylationQLVKTYEYKKAEERE
HHHHHCCHHCHHHCC		13.8429759185
198UbiquitinationPDSSYYSVLLQKQIL
CCCCHHHHHHHHHHH		3.4129967540
202UbiquitinationYYSVLLQKQILKIFY
HHHHHHHHHHHHHHH		39.00-
253UbiquitinationLHIDEDDRPELVWWK
CCCCCCCCCHHHHHH		38.6224816145
284UbiquitinationGSPGNVTKEYFEFSE
CCCCCCCHHHHHHHH		46.24-
298UbiquitinationEFFLKTYAVGIQQVL
HHHHHHHHHHHHHHH		9.7833845483
305UbiquitinationAVGIQQVLLKILDQY
HHHHHHHHHHHHHHH		3.3321890473
310UbiquitinationQVLLKILDQYRQKEY
HHHHHHHHHHHCCCC		47.1122817900
315UbiquitinationILDQYRQKEYVAPRV
HHHHHHCCCCCHHHH		41.8524816145
329PhosphorylationVLQQAFNYLNQGVVH
HHHHHHHHHHHCCCC		10.6925867546
337PhosphorylationLNQGVVHSITWKQMK
HHHCCCCEEEHHHCC		15.3125867546
339PhosphorylationQGVVHSITWKQMKPH
HCCCCEEEHHHCCHH		29.6225867546
374PhosphorylationELWQEDPYEYIRMKF
HHHCCCHHHHHHHHH		33.42-
380UbiquitinationPYEYIRMKFDIFEDY
HHHHHHHHHHHCCCC		30.00-
387PhosphorylationKFDIFEDYASPTTAA
HHHHCCCCCCHHHHH		11.2023401153
389PhosphorylationDIFEDYASPTTAAQT
HHCCCCCCHHHHHHH		19.2917192257
391PhosphorylationFEDYASPTTAAQTLL
CCCCCCHHHHHHHHH		26.9423401153
392PhosphorylationEDYASPTTAAQTLLY
CCCCCHHHHHHHHHH		24.3123401153
399PhosphorylationTAAQTLLYTAAKKRK
HHHHHHHHHHHHHHH		9.4623401153
403UbiquitinationTLLYTAAKKRKEVLP
HHHHHHHHHHHHHHH		51.1229967540
439PhosphorylationGALHVIGSLAEILLK
CHHHHHHHHHHHHHH		17.1824114839
448UbiquitinationAEILLKKSLFKDQME
HHHHHHHHCCHHHHH		37.1321890473
448PhosphorylationAEILLKKSLFKDQME
HHHHHHHHCCHHHHH		37.1324719451
453UbiquitinationKKSLFKDQMELFLQN
HHHCCHHHHHHHHHH		28.0422817900
493UbiquitinationSLKFHNELNLRNAVE
HCCCCCHHCHHHHHH		9.9321890473
498UbiquitinationNELNLRNAVELAKKS
CHHCHHHHHHHHHHH		6.9622817900
503UbiquitinationRNAVELAKKSLIEDK
HHHHHHHHHHCCCCC		56.3633845483
504UbiquitinationNAVELAKKSLIEDKE
HHHHHHHHHCCCCCC		44.91-
510UbiquitinationKKSLIEDKEMPVKVE
HHHCCCCCCCCHHHH		43.0221890473
510UbiquitinationKKSLIEDKEMPVKVE
HHHCCCCCCCCHHHH		43.0221906983
515UbiquitinationEDKEMPVKVEAALAL
CCCCCCHHHHHHHHH		28.6122817900
524PhosphorylationEAALALQSLISNQIQ
HHHHHHHHHHHCCHH		28.64-
527PhosphorylationLALQSLISNQIQAKE
HHHHHHHHCCHHHHH		28.16-
535PhosphorylationNQIQAKEYMKPHVRP
CCHHHHHHCCHHHHH		15.1025332170
565AcetylationDVTNVIQKMICEYSQ
HHHHHHHHHHHHHHH		21.0719813079
595PhosphorylationIFGKVLQSDEYEEVE
HHHHHHCCCCCHHCC		28.4025627689
598PhosphorylationKVLQSDEYEEVEDKT
HHHCCCCCHHCCCHH		23.5228796482
705PhosphorylationHNYVTIDTDTLLSNA
CCCEEECHHHHHHCC		27.3426074081
707PhosphorylationYVTIDTDTLLSNAKH
CEEECHHHHHHCCHH		31.5226074081
710PhosphorylationIDTDTLLSNAKHLEI
ECHHHHHHCCHHHHH		37.5426074081
720PhosphorylationKHLEILFTMCRKVLC
HHHHHHHHHHCHHHC		16.3626074081
804UbiquitinationLLHTLERIQLPHNPG
HHHHHHHCCCCCCCC		3.4429967540
805UbiquitinationLHTLERIQLPHNPGP
HHHHHHCCCCCCCCC		55.9829967540
902PhosphorylationMEENEEISSDEEETN
HHHHCCCCCCCHHHH		34.7122167270
903PhosphorylationEENEEISSDEEETNV
HHHCCCCCCCHHHHH		55.4922167270
908PhosphorylationISSDEEETNVTAQAM
CCCCCHHHHHHHHHH		37.9622167270
911PhosphorylationDEEETNVTAQAMQSN
CCHHHHHHHHHHHHC		18.3422167270
917PhosphorylationVTAQAMQSNNGRGED
HHHHHHHHCCCCCCC		21.1222167270
995PhosphorylationRTALQEVYTLAEHRR
HHHHHHHHHHHHHHH		8.6927642862
1003PhosphorylationTLAEHRRTVAEAKKK
HHHHHHHHHHHHHHH		24.8321406692
1009UbiquitinationRTVAEAKKKIEQQGG
HHHHHHHHHHHHCCC		67.0629967540
1010UbiquitinationTVAEAKKKIEQQGGF
HHHHHHHHHHHCCCC		51.2529967540
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 IPO8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IPO8_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 IPO8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AGO1_HUMANAGO1physical
19167051
AGO2_HUMANAGO2physical
19167051
AGO3_HUMANAGO3physical
19167051
AGO4_HUMANAGO4physical
19167051
IPO9_HUMANIPO9physical
26344197
PPM1G_HUMANPPM1Gphysical
26344197
BIN1_HUMANBIN1physical
26496610
CBLB_HUMANCBLBphysical
26496610
RA51D_HUMANRAD51Dphysical
26496610
ZNF7_HUMANZNF7physical
26496610
TIF1B_HUMANTRIM28physical
26496610
ZN629_HUMANZNF629physical
26496610
ACAD8_HUMANACAD8physical
26496610
REPI1_HUMANREPIN1physical
26496610
BCOR_HUMANBCORphysical
26496610
ZN331_HUMANZNF331physical
26496610
ZBT10_HUMANZBTB10physical
26496610
ZN696_HUMANZNF696physical
26496610
OSBL5_HUMANOSBPL5physical
26496610
ZFP1_HUMANZFP1physical
26496610
ZSC25_HUMANZSCAN25physical
26496610
STOM_HUMANSTOMphysical
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 IPO8_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902 AND SER-903, ANDMASS SPECTROMETRY.
"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 SER-902 AND SER-903, ANDMASS SPECTROMETRY.
"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-389; SER-902 ANDSER-903, AND MASS SPECTROMETRY.

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