TNPO2_HUMAN - dbPTM
TNPO2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TNPO2_HUMAN
UniProt AC O14787
Protein Name Transportin-2
Gene Name TNPO2
Organism Homo sapiens (Human).
Sequence Length 897
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Probably 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)..
Protein Sequence MDWQPDEQGLQQVLQLLKDSQSPNTATQRIVQDKLKQLNQFPDFNNYLIFVLTRLKSEDEPTRSLSGLILKNNVKAHYQSFPPPVADFIKQECLNNIGDASSLIRATIGILITTIASKGELQMWPELLPQLCNLLNSEDYNTCEGAFGALQKICEDSSELLDSDALNRPLNIMIPKFLQFFKHCSPKIRSHAIACVNQFIMDRAQALMDNIDTFIEHLFALAVDDDPEVRKNVCRALVMLLEVRIDRLIPHMHSIIQYMLQRTQDHDENVALEACEFWLTLAEQPICKEVLASHLVQLIPILVNGMKYSEIDIILLKGDVEEDEAVPDSEQDIKPRFHKSRTVTLPHEAERPDGSEDAEDDDDDDALSDWNLRKCSAAALDVLANVFREELLPHLLPLLKGLLFHPEWVVKESGILVLGAIAEGCMQGMVPYLPELIPHLIQCLSDKKALVRSIACWTLSRYAHWVVSQPPDMHLKPLMTELLKRILDGNKRVQEAACSAFATLEEEACTELVPYLSYILDTLVFAFGKYQHKNLLILYDAIGTLADSVGHHLNQPEYIQKLMPPLIQKWNELKDEDKDLFPLLECLSSVATALQSGFLPYCEPVYQRCVTLVQKTLAQAMMYTQHPEQYEAPDKDFMIVALDLLSGLAEGLGGHVEQLVARSNIMTLLFQCMQDSMPEVRQSSFALLGDLTKACFIHVKPCIAEFMPILGTNLNPEFISVCNNATWAIGEICMQMGAEMQPYVQMVLNNLVEIINRPNTPKTLLENTGRLTSPSAIPAITIGRLGYVCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICMMIGVNPGGVVQDFIFFCDAVASWVSPKDDLRDMFYKILHGFKDQVGEDNWQQFSEQFPPLLKERLAAFYGV
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
25PhosphorylationKDSQSPNTATQRIVQ
HCCCCCCHHHHHHHH		34.17-
34UbiquitinationTQRIVQDKLKQLNQF
HHHHHHHHHHHHHCC		40.26-
57PhosphorylationFVLTRLKSEDEPTRS
HHHHCCCCCCCCCCC		55.6721406692
57 (in isoform 2)Phosphorylation-55.6721406692
64PhosphorylationSEDEPTRSLSGLILK
CCCCCCCCCCCCHHH		29.3921406692
64 (in isoform 2)Phosphorylation-29.3921406692
66PhosphorylationDEPTRSLSGLILKNN
CCCCCCCCCCHHHCC		32.5730108239
71 (in isoform 2)Ubiquitination-39.2121890473
71MalonylationSLSGLILKNNVKAHY
CCCCCHHHCCHHHHH		39.2133225896
71AcetylationSLSGLILKNNVKAHY
CCCCCHHHCCHHHHH		39.2125953088
71 (in isoform 1)Ubiquitination-39.2121890473
71UbiquitinationSLSGLILKNNVKAHY
CCCCCHHHCCHHHHH		39.2121906983
75UbiquitinationLILKNNVKAHYQSFP
CHHHCCHHHHHHCCC		31.41-
102PhosphorylationNNIGDASSLIRATIG
HHCCCHHHHHHHHHH		29.5424719451
182AcetylationPKFLQFFKHCSPKIR
HHHHHHHHHCCHHHH		45.0225953088
254PhosphorylationRLIPHMHSIIQYMLQ
HHHHHHHHHHHHHHH		17.5130631047
258PhosphorylationHMHSIIQYMLQRTQD
HHHHHHHHHHHHCCC		6.8730631047
334 (in isoform 2)Ubiquitination-38.1321890473
334UbiquitinationPDSEQDIKPRFHKSR
CCCHHCCCCCCCCCC		38.1321906983
334 (in isoform 1)Ubiquitination-38.1321890473
340PhosphorylationIKPRFHKSRTVTLPH
CCCCCCCCCEEECCC		25.3121406692
342PhosphorylationPRFHKSRTVTLPHEA
CCCCCCCEEECCCCC		25.5720873877
344PhosphorylationFHKSRTVTLPHEAER
CCCCCEEECCCCCCC		33.6820873877
355 (in isoform 2)Phosphorylation-39.4221406692
355PhosphorylationEAERPDGSEDAEDDD
CCCCCCCCCCCCCCC		39.4223898821
368PhosphorylationDDDDDALSDWNLRKC
CCCCCCHHHHHHHHH		42.1520873877
374UbiquitinationLSDWNLRKCSAAALD
HHHHHHHHHHHHHHH		35.39-
376PhosphorylationDWNLRKCSAAALDVL
HHHHHHHHHHHHHHH		24.7924114839
458PhosphorylationVRSIACWTLSRYAHW
HHHHHHHHHHHHCHH		18.1020071362
484 (in isoform 1)Ubiquitination-50.4421890473
484 (in isoform 2)Ubiquitination-50.4421890473
484UbiquitinationPLMTELLKRILDGNK
HHHHHHHHHHHCCCH		50.4421890473
484UbiquitinationPLMTELLKRILDGNK
HHHHHHHHHHHCCCH		50.44-
683PhosphorylationSMPEVRQSSFALLGD
CCHHHHHHHHHHHHH		19.5021712546
684PhosphorylationMPEVRQSSFALLGDL
CHHHHHHHHHHHHHH		13.2421712546
760PhosphorylationEIINRPNTPKTLLEN
HHHCCCCCCCHHHHH		28.9225599653
817AcetylationNIRDNEEKDSAFRGI
CCCCCCCCCCHHHHH		51.2926822725
817UbiquitinationNIRDNEEKDSAFRGI
CCCCCCCCCCHHHHH		51.29-
852 (in isoform 2)Acetylation-34.18-
862UbiquitinationDLRDMFYKILHGFKD
HHHHHHHHHHHHCHH		27.762189047
862AcetylationDLRDMFYKILHGFKD
HHHHHHHHHHHHCHH		27.7619608861
868UbiquitinationYKILHGFKDQVGEDN
HHHHHHCHHCCCCCC		52.41-
888UbiquitinationEQFPPLLKERLAAFY
HHCCHHHHHHHHHHH		48.77-
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 TNPO2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TNPO2_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 TNPO2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A1CF_HUMANA1CFphysical
12896982
NUP98_HUMANNUP98physical
10875935
NXF1_HUMANNXF1physical
12384575
MTNB_HUMANAPIPphysical
25416956
CA094_HUMANC1orf94physical
25416956
PNMA5_HUMANPNMA5physical
25416956
TBB5_HUMANTUBBphysical
26344197
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 TNPO2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-862, AND MASS SPECTROMETRY.

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