IPO9_HUMAN - dbPTM
IPO9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IPO9_HUMAN
UniProt AC Q96P70
Protein Name Importin-9
Gene Name IPO9
Organism Homo sapiens (Human).
Sequence Length 1041
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 (By similarity). Mediates the nuclear import of H2B histone (By similarity), RPS7 and RPL18A. Prevents the cytoplasmic aggregation of RPS7 and RPL18A by shielding exposed basic domains. May also import H2A, H3, H4 histones (By similarity), RPL4 and RPL6..
Protein Sequence MAAAAAAGAASGLPGPVAQGLKEALVDTLTGILSPVQEVRAAAEEQIKVLEVTEEFGVHLAELTVDPQGALAIRQLASVILKQYVETHWCAQSEKFRPPETTERAKIVIRELLPNGLRESISKVRSSVAYAVSAIAHWDWPEAWPQLFNLLMEMLVSGDLNAVHGAMRVLTEFTREVTDTQMPLVAPVILPEMYKIFTMAEVYGIRTRSRAVEIFTTCAHMICNMEELEKGAAKVLIFPVVQQFTEAFVQALQIPDGPTSDSGFKMEVLKAVTALVKNFPKHMVSSMQQILPIVWNTLTESAAFYVRTEVNYTEEVEDPVDSDGEVLGFENLVFSIFEFVHALLENSKFKSTVKKALPELIYYIILYMQITEEQIKVWTANPQQFVEDEDDDTFSYTVRIAAQDLLLAVATDFQNESAAALAAAATRHLQEAEQTKNSGTEHWWKIHEACMLALGSVKAIITDSVKNGRIHFDMHGFLTNVILADLNLSVSPFLLGRALWAASRFTVAMSPELIQQFLQATVSGLHETQPPSVRISAVRAIWGYCDQLKVSESTHVLQPFLPSILDGLIHLAAQFSSEVLNLVMETLCIVCTVDPEFTASMESKICPFTIAIFLKYSNDPVVASLAQDIFKELSQIEACQGPMQMRLIPTLVSIMQAPADKIPAGLCATAIDILTTVVRNTKPPLSQLLICQAFPAVAQCTLHTDDNATMQNGGECLRAYVSVTLEQVAQWHDEQGHNGLWYVMQVVSQLLDPRTSEFTAAFVGRLVSTLISKAGRELGENLDQILRAILSKMQQAETLSVMQSLIMVFAHLVHTQLEPLLEFLCSLPGPTGKPALEFVMAEWTSRQHLFYGQYEGKVSSVALCKLLQHGINADDKRLQDIRVKGEEIYSMDEGIRTRSKSAKNPERWTNIPLLVKILKLIINELSNVMEANAARQATPAEWSQDDSNDMWEDQEEEEEEEEDGLAGQLLSDILATSKYEEDYYEDDEEDDPDALKDPLYQIDLQAYLTDFLCQFAQQPCYIMFSGHLNDNERRVLQTIGI
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------MAAAAAAGA
------CHHHHHHHH		19.6722223895
34PhosphorylationDTLTGILSPVQEVRA
HHHHHCCCHHHHHHH		22.5430377224
82AcetylationQLASVILKQYVETHW
HHHHHHHHHHHHHCC		28.5825953088
95UbiquitinationHWCAQSEKFRPPETT
CCCCCCCCCCCCCCH		52.5029967540
95AcetylationHWCAQSEKFRPPETT
CCCCCCCCCCCCCCH		52.5025953088
102PhosphorylationKFRPPETTERAKIVI
CCCCCCCHHHHHHHH		23.0828787133
123UbiquitinationGLRESISKVRSSVAY
CHHHHHHHHHHHHHH		39.7424816145
178PhosphorylationTEFTREVTDTQMPLV
HHHHCCCCCCCCCCC		28.6920068231
180PhosphorylationFTREVTDTQMPLVAP
HHCCCCCCCCCCCCC		19.8720068231
194PhosphorylationPVILPEMYKIFTMAE
CCCCHHHHHHHHHHH		10.1622210691
199SulfoxidationEMYKIFTMAEVYGIR
HHHHHHHHHHHHCCC		1.7728183972
203PhosphorylationIFTMAEVYGIRTRSR
HHHHHHHHCCCCCCH		9.80-
265UbiquitinationPTSDSGFKMEVLKAV
CCCCCCHHHHHHHHH		37.3622817900
270UbiquitinationGFKMEVLKAVTALVK
CHHHHHHHHHHHHHH		46.0921906983
277MalonylationKAVTALVKNFPKHMV
HHHHHHHHCCCHHHH		54.4426320211
277UbiquitinationKAVTALVKNFPKHMV
HHHHHHHHCCCHHHH		54.4433845483
277AcetylationKAVTALVKNFPKHMV
HHHHHHHHCCCHHHH		54.4423236377
322PhosphorylationEVEDPVDSDGEVLGF
ECCCCCCCCCCCCCH		47.9920068231
435PhosphorylationHLQEAEQTKNSGTEH
HHHHHHHHCCCCCCC		24.57-
436UbiquitinationLQEAEQTKNSGTEHW
HHHHHHHCCCCCCCH		49.1322817900
466UbiquitinationAIITDSVKNGRIHFD
EEEECCHHHCEEEEE		58.6027667366
489PhosphorylationILADLNLSVSPFLLG
HHHCCCCCCCHHHHH		21.34-
768PhosphorylationAFVGRLVSTLISKAG
HHHHHHHHHHHHHHH		23.3021406692
769PhosphorylationFVGRLVSTLISKAGR
HHHHHHHHHHHHHHH		22.1920068231
772PhosphorylationRLVSTLISKAGRELG
HHHHHHHHHHHHHHH		21.4021406692
773UbiquitinationLVSTLISKAGRELGE
HHHHHHHHHHHHHHH		48.1121906983
865UbiquitinationVSSVALCKLLQHGIN
CHHHHHHHHHHCCCC		53.7522817900
8762-HydroxyisobutyrylationHGINADDKRLQDIRV
CCCCCCCCCHHHCEE		56.40-
876UbiquitinationHGINADDKRLQDIRV
CCCCCCCCCHHHCEE		56.4029967540
884UbiquitinationRLQDIRVKGEEIYSM
CHHHCEECCCEEEEC		51.2421906983
889PhosphorylationRVKGEEIYSMDEGIR
EECCCEEEECCCCHH		10.9621945579
890PhosphorylationVKGEEIYSMDEGIRT
ECCCEEEECCCCHHC		25.9721945579
891SulfoxidationKGEEIYSMDEGIRTR
CCCEEEECCCCHHCC		2.8230846556
897PhosphorylationSMDEGIRTRSKSAKN
ECCCCHHCCCCCCCC		37.0624173317
900UbiquitinationEGIRTRSKSAKNPER
CCHHCCCCCCCCHHH		51.6624816145
909PhosphorylationAKNPERWTNIPLLVK
CCCHHHHCCHHHHHH		29.50-
929SulfoxidationINELSNVMEANAARQ
HHHHHHHHHHHHHHH		4.7521406390
938PhosphorylationANAARQATPAEWSQD
HHHHHHCCCCCCCCC		18.0718691976
947PhosphorylationAEWSQDDSNDMWEDQ
CCCCCCCCCCCCCCH		42.9117192257
971PhosphorylationGLAGQLLSDILATSK
CHHHHHHHHHHHHCC		31.0617192257
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 IPO9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IPO9_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 IPO9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
NP1L1_HUMANNAP1L1physical
22939629
GNPI1_HUMANGNPDA1physical
22863883
HMGB3_HUMANHMGB3physical
22863883
NOL3_HUMANNOL3physical
22863883
PLIN3_HUMANPLIN3physical
22863883
TNPO1_HUMANTNPO1physical
22863883
IPO7_HUMANIPO7physical
26344197
RPN1_HUMANRPN1physical
26344197
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 IPO9_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 ALA-2, AND MASS SPECTROMETRY.

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