IPO11_HUMAN - dbPTM
IPO11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IPO11_HUMAN
UniProt AC Q9UI26
Protein Name Importin-11
Gene Name IPO11
Organism Homo sapiens (Human).
Sequence Length 975
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 UBE2E3, and of RPL12 (By similarity)..
Protein Sequence MDLNSASTVVLQVLTQATSQDTAVLKPAEEQLKQWETQPGFYSVLLNIFTNHTLDINVRWLAVLYFKHGIDRYWRRVAPHALSEEEKTTLRAGLITNFNEPINQIATQIAVLIAKVARLDCPRQWPELIPTLIESVKVQDDLRQHRALLTFYHVTKTLASKRLAADRKLFYDLASGIYNFACSLWNHHTDTFLQEVSSGNEAAILSSLERTLLSLKVLRKLTVNGFVEPHKNMEVMGFLHGIFERLKQFLECSRSIGTDNVCRDRLEKTIILFTKVLLDFLDQHPFSFTPLIQRSLEFSVSYVFTEVGEGVTFERFIVQCMNLIKMIVKNYAYKPSKNFEDSSPETLEAHKIKMAFFTYPTLTEICRRLVSHYFLLTEEELTMWEEDPEGFTVEETGGDSWKYSLRPCTEVLFIDIFHEYNQTLTPVLLEMMQTLQGPTNVEDMNALLIKDAVYNAVGLAAYELFDSVDFDQWFKNQLLPELQVIHNRYKPLRRRVIWLIGQWISVKFKSDLRPMLYEAICNLLQDQDLVVRIETATTLKLTVDDFEFRTDQFLPYLETMFTLLFQLLQQVTECDTKMHVLHVLSCVIERVNMQIRPYVGCLVQYLPLLWKQSEEHNMLRCAILTTLIHLVQGLGADSKNLYPFLLPVIQLSTDVSQPPHVYLLEDGLELWLVTLENSPCITPELLRIFQNMSPLLELSSENLRTCFKIINGYIFLSSTEFLQTYAVGLCQSFCELLKEITTEGQVQVLKVVENALKVNPILGPQMFQPILPYVFKGIIEGERYPVVMSTYLGVMGRVLLQNTSFFSSLLNEMAHKFNQEMDQLLGNMIEMWVDRMDNITQPERRKLSALALLSLLPSDNSVIQDKFCGIINISVEGLHDVMTEDPETGTYKDCMLMSHLEEPKVTEDEEPPTEQDKRKKMLALKDPVHTVSLQQFIYEKLKAQQEMLGEQGFQSLMETVDTEIVTQLQEFLQGF
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-------MDLNSAST
-------CCHHHHHH		13.7619413330
5Phosphorylation---MDLNSASTVVLQ
---CCHHHHHHHHHH		30.7830576142
7Phosphorylation-MDLNSASTVVLQVL
-CCHHHHHHHHHHHH		22.8930576142
8PhosphorylationMDLNSASTVVLQVLT
CCHHHHHHHHHHHHH		17.8524043423
10 (in isoform 2)Phosphorylation-2.9124043423
13 (in isoform 2)Phosphorylation-5.6624043423
14 (in isoform 2)Phosphorylation-1.5724043423
15PhosphorylationTVVLQVLTQATSQDT
HHHHHHHHHCCCCCC		19.8024043423
17 (in isoform 2)Phosphorylation-12.1824043423
18PhosphorylationLQVLTQATSQDTAVL
HHHHHHCCCCCCEEC		19.6630576142
19PhosphorylationQVLTQATSQDTAVLK
HHHHHCCCCCCEECC		29.1324043423
20 (in isoform 2)Phosphorylation-47.9524043423
22PhosphorylationTQATSQDTAVLKPAE
HHCCCCCCEECCHHH		15.8424043423
83PhosphorylationRVAPHALSEEEKTTL
HHCHHCCCHHHHHHH		43.6920068231
87UbiquitinationHALSEEEKTTLRAGL
HCCCHHHHHHHHHHH		50.5224816145
127UbiquitinationDCPRQWPELIPTLIE
CCCCCCCHHHHHHHH		57.2724816145
161UbiquitinationVTKTLASKRLAADRK
HHHHHHHHHHHHCHH		45.9127667366
201UbiquitinationQEVSSGNEAAILSSL
HHHHCCCHHHHHHHH		42.9027667366
206PhosphorylationGNEAAILSSLERTLL
CCHHHHHHHHHHHHH		27.1124719451
214PhosphorylationSLERTLLSLKVLRKL
HHHHHHHHHHHHHHH		29.2924719451
216UbiquitinationERTLLSLKVLRKLTV
HHHHHHHHHHHHHCC		35.5323000965
220UbiquitinationLSLKVLRKLTVNGFV
HHHHHHHHHCCCCEE		44.3323000965
247UbiquitinationHGIFERLKQFLECSR
HHHHHHHHHHHHHHH		45.2724816145
256UbiquitinationFLECSRSIGTDNVCR
HHHHHHHHCCCCHHH		7.1821890473
256UbiquitinationFLECSRSIGTDNVCR
HHHHHHHHCCCCHHH		7.1821890473
256 (in isoform 2)Ubiquitination-7.18-
260UbiquitinationSRSIGTDNVCRDRLE
HHHHCCCCHHHHHHH		34.3323000965
287UbiquitinationFLDQHPFSFTPLIQR
HHHHCCCCCHHHHHH		32.4424816145
305PhosphorylationFSVSYVFTEVGEGVT
EEEEEEEEECCCCCC		21.5119053533
312PhosphorylationTEVGEGVTFERFIVQ
EECCCCCCHHHHHHH		30.5419053533
334UbiquitinationIVKNYAYKPSKNFED
HHHHCCCCCCCCCCC		34.3427667366
337UbiquitinationNYAYKPSKNFEDSSP
HCCCCCCCCCCCCCH		74.3429967540
342PhosphorylationPSKNFEDSSPETLEA
CCCCCCCCCHHHHHH		40.3629255136
343PhosphorylationSKNFEDSSPETLEAH
CCCCCCCCHHHHHHH		38.7929255136
346PhosphorylationFEDSSPETLEAHKIK
CCCCCHHHHHHHHCE		33.0323663014
351AcetylationPETLEAHKIKMAFFT
HHHHHHHHCEEHHHC		51.5825953088
351UbiquitinationPETLEAHKIKMAFFT
HHHHHHHHCEEHHHC		51.5829967540
361PhosphorylationMAFFTYPTLTEICRR
EHHHCCHHHHHHHHH		35.58-
374UbiquitinationRRLVSHYFLLTEEEL
HHHHHHHHCCCHHHH		3.6427667366
377UbiquitinationVSHYFLLTEEELTMW
HHHHHCCCHHHHHCC		43.4229967540
383PhosphorylationLTEEELTMWEEDPEG
CCHHHHHCCCCCCCC		7.1027251275
391UbiquitinationWEEDPEGFTVEETGG
CCCCCCCCEEEECCC		7.0629967540
404PhosphorylationGGDSWKYSLRPCTEV
CCCCCEEECCCCCEE		17.7424719451
540UbiquitinationIETATTLKLTVDDFE
EEECCEEEEEECCCC		39.7729901268
580UbiquitinationECDTKMHVLHVLSCV
HCCCHHHHHHHHHHH		3.3729901268
784PhosphorylationGIIEGERYPVVMSTY
HHHCCCCCCCHHHHH		8.9720068231
846UbiquitinationITQPERRKLSALALL
CCCHHHHHHHHHHHH		53.68-
854PhosphorylationLSALALLSLLPSDNS
HHHHHHHHCCCCCCH		28.8020860994
858PhosphorylationALLSLLPSDNSVIQD
HHHHCCCCCCHHHCC		49.7720860994
861PhosphorylationSLLPSDNSVIQDKFC
HCCCCCCHHHCCCCC		26.1120860994
898PhosphorylationYKDCMLMSHLEEPKV
HHHCHHHHCCCCCCC		22.4328555341
917UbiquitinationEPPTEQDKRKKMLAL
CCCCHHHHHHHHHHH		66.8521890473
940UbiquitinationLQQFIYEKLKAQQEM
HHHHHHHHHHHHHHH		38.0129967540
980UbiquitinationQGF------------
CCC------------		29967540
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 IPO11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IPO11_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 IPO11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLCD4_HUMANPLCD4physical
16189514
RL12_HUMANRPL12physical
11809816
RAN_HUMANRANphysical
11032817
UB2E1_HUMANUBE2E1physical
11032817
UB2E3_HUMANUBE2E3physical
15545318
UB2E1_HUMANUBE2E1physical
15545318
UB2E2_HUMANUBE2E2physical
15545318
NXF1_HUMANNXF1physical
21965294
SH3G2_HUMANSH3GL2physical
22939629
SYAC_HUMANAARSphysical
22863883
CYBP_HUMANCACYBPphysical
22863883
NC2B_HUMANDR1physical
22863883
IF4A3_HUMANEIF4A3physical
22863883
HNRPD_HUMANHNRNPDphysical
22863883
HNRH1_HUMANHNRNPH1physical
22863883
PDLI5_HUMANPDLIM5physical
22863883
KPYM_HUMANPKMphysical
22863883
PLIN3_HUMANPLIN3physical
22863883
PRDX2_HUMANPRDX2physical
22863883
RAGP1_HUMANRANGAP1physical
22863883
SRP09_HUMANSRP9physical
22863883
TPRKB_HUMANTPRKBphysical
22863883
CA094_HUMANC1orf94physical
25416956
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 IPO11_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.

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